Affinage

TUFM

Elongation factor Tu, mitochondrial · UniProt P49411

Length
455 aa
Mass
49.9 kDa
Annotated
2026-06-10
100 papers in source corpus 30 papers cited in narrative 30 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 5/5 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TUFM is the mitochondrial Tu translation elongation factor, a conserved three-domain GTPase whose GDP→GTP transition drives a ~90° rotation of domain 1 to expose the aminoacyl-tRNA binding cleft, delivering aminoacyl-tRNAs to the ribosomal A-site during translation elongation (PMID:8069622, PMID:10715211); the mammalian mitochondrial ortholog retains this architecture but binds nucleotide less tightly and carries a C-terminal extension implicated in RNA recognition (PMID:10715211). TUFM is essential for mitochondrial DNA translation in vivo, and its loss or overexpression directly modulates translation fidelity and respiratory chain assembly: biallelic TUFM mutations cause severe infantile lactic acidosis, fatal encephalopathy, and leukodystrophy with defective mitochondrial translation (PMID:17160893), and raising TUFM levels suppresses translation defects in MELAS mutant cells (PMID:18753147). Beyond translation, TUFM has a non-canonical role at the outer mitochondrial membrane as a scaffold for autophagy and mitophagy: it self-dimerizes via an N-terminal GxxxG motif (PMID:34511600) and assembles with NLRX1 and the Atg5-Atg12/Atg16L1 machinery to promote autophagy while dampening RLR/RIG-I-driven type I interferon responses during viral infection (PMID:22749352, PMID:23321557). It recruits Beclin-1 to mitochondria and displaces it from Rubicon to enhance autophagic flux (PMID:26876213), and acts in a Parkin-independent mitophagy route governed by a PINK1-catalyzed Ser222 phosphoswitch that converts membrane-bound TUFM from a mitophagy activator into a cytosolic inhibitor (PMID:33113344). This mitophagic output is further tuned by post-translational modifications—K82/K91 deacetylation by MRG15 targeting TUFM for ClpXP degradation (PMID:35985547), K286 lactylation blocking its TOMM40 interaction and mitochondrial distribution (PMID:39496783), and RNF185-catalyzed K27-linked ubiquitination that recruits SQSTM1/LC3 (PMID:38084826)—with downstream consequences for apoptosis, innate immunity, and metabolic homeostasis (PMID:34511600, PMID:33398033).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 1992 High

    Establishing the inactive GDP-bound conformation defined the structural ground state of the elongation factor and its GDP-binding site.

    Evidence X-ray crystallography of E. coli EF-Tu·GDP at 2.6 Å

    PMID:1542116

    Open questions at the time
    • Bacterial ortholog, not mammalian mitochondrial TUFM
    • Does not show the active conformation or tRNA engagement
  2. 1995 High

    Capturing the ternary complex showed how the GTP-bound factor cradles aminoacyl-tRNA, defining the molecular basis of tRNA delivery and 'molecular mimicry'.

    Evidence X-ray crystallography of Phe-tRNA·EF-Tu·GDPNP at 2.7 Å

    PMID:7491491

    Open questions at the time
    • Bacterial ortholog
    • Static snapshot does not resolve hydrolysis dynamics
  3. 1997 Medium

    Cloning the human gene and resolving the EF-Tu·EF-Ts exchange complex established TUFM's molecular identity and the nucleotide exchange mechanism that recycles it.

    Evidence cDNA cloning/chromosomal mapping of human TUFM; X-ray crystallography of EF-Tu·EF-Ts

    PMID:9253415 PMID:9332382

    Open questions at the time
    • Exchange structure is bacterial
    • Human EF-Ts (TSFM) interaction not structurally validated for TUFM
  4. 2000 High

    The mammalian mitochondrial TUFM structure showed it retains the EF-Tu fold but with altered domain orientation, weaker nucleotide binding, and a C-terminal extension implicated in RNA recognition.

    Evidence X-ray crystallography of bovine TUFM·GDP at 1.94 Å

    PMID:10715211

    Open questions at the time
    • GTP-bound mitochondrial form not solved
    • RNA-recognition role of C-terminal extension inferred, not demonstrated
  5. 2006 High

    Patient mutations linked TUFM directly to human disease and demonstrated its essential role in mitochondrial translation via cross-species complementation.

    Evidence Functional complementation in yeast and mammalian cells from patients with lactic acidosis and encephalopathy

    PMID:17160893

    Open questions at the time
    • Does not address non-translational functions
    • Genotype-phenotype range incompletely mapped
  6. 2008 High

    Showing that TUFM levels modulate translation fidelity in MELAS cells established that the factor is rate-limiting for mitochondrial protein synthesis quality.

    Evidence Overexpression rescue, BN-PAGE, pulse-chase, and misincorporation analysis in mutant myoblasts

    PMID:18753147

    Open questions at the time
    • Mechanism of misincorporation suppression not fully defined
  7. 2012 High

    Identifying TUFM as an NLRX1 partner that links to Atg5-Atg12/Atg16L1 revealed an unanticipated moonlighting role bridging mitochondria, autophagy, and innate immune restraint.

    Evidence Quantitative mass spectrometry, endogenous co-IP, and KO/KD functional assays during viral infection

    PMID:22749352

    Open questions at the time
    • How a translation factor is recruited to the autophagy machinery unresolved
    • Topology relative to inner vs outer membrane unclear at this stage
  8. 2016 Medium

    Mechanistic dissection showed TUFM anchors Beclin-1 to mitochondria and antagonizes Rubicon to promote flux, while also suppressing an AMPK-GSK3β-β-catenin axis to maintain epithelial phenotype.

    Evidence Co-IP, ubiquitination and autophagic flux assays in HNSCC cells; siRNA knockdown with pathway readouts in A549 cells

    PMID:26781467 PMID:26876213

    Open questions at the time
    • Single-lab findings
    • Direct vs indirect Beclin-1 binding not separated from scaffold effect
  9. 2020 High

    Discovery of the PINK1-driven Ser222 phosphoswitch and dual mitochondrial/cytosolic localization explained how TUFM is toggled between mitophagy activator and inhibitor in a Parkin-independent route.

    Evidence Co-IP, S222A/S222E mutagenesis, fractionation, live imaging, genetic epistasis, in vitro kinase assays

    PMID:33113344

    Open questions at the time
    • Cytosolic pool's relationship to translation pool unclear
    • Phosphatase reversing S222 not identified
  10. 2021 High

    Defining the OMM-localized, GxxxG-dependent dimer linked TUFM's autophagic activity to suppression of caspase-8 apoptosis and to ROS-dependent control of disease pathways.

    Evidence Inducible KD, fractionation, GxxxG mutagenesis, apoptosis assays; DARTS/MS kaempferide target ID; mRNA-stability and ROS assays in HEK-APP cells

    PMID:33398033 PMID:33774866 PMID:34511600

    Open questions at the time
    • How dimerization couples to autophagy machinery mechanistically unclear
    • ROS-sensing step upstream of these outputs undefined
  11. 2022 Medium

    Two studies established PTM and partner control of TUFM stability and mtDNA integrity: MRG15 deacetylation routes TUFM to ClpXP degradation, and FUNDC1 binding maintains mtDNA stability against cytosolic release.

    Evidence IP-MS, acetylation-site mutagenesis, ClpXP protease assay, in vivo CRISPR (NASH); domain-mapped co-IP and mtDNA release/PANoptosis assays

    PMID:35985547 PMID:36470869

    Open questions at the time
    • FUNDC1 study single-lab
    • Acetyltransferase opposing MRG15 not defined
  12. 2024 High

    Lactylation and viral-driven ubiquitination revealed additional layers tuning TUFM's mitophagic output, and showed pathogens hijack TUFM-dependent mitophagy to evade immunity.

    Evidence K286R knockin and lactylation MS (TBI model); RNF185 K27-ubiquitination with SQSTM1/LC3 recruitment (SVA); SFTSV-NP and influenza PB2 interaction with mitophagy/MAVS readouts

    PMID:28611246 PMID:38084826 PMID:39189526 PMID:39496783

    Open questions at the time
    • Interplay among competing PTMs (lactylation, ubiquitination, acetylation, phosphorylation) not integrated
    • Whether viral hijacking uses the same residues as physiological mitophagy unclear

Open questions

Synthesis pass · forward-looking unresolved questions
  • How TUFM's canonical translation function is physically and regulatorily coordinated with its OMM scaffolding role, and how the various PTM inputs are hierarchically integrated, remains unresolved.
  • No structure of mammalian TUFM in any autophagy complex
  • Quantitative partitioning between translation, OMM, and cytosolic pools unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 2 GO:0003924 GTPase activity 2 GO:0045182 translation regulator activity 2 GO:0060090 molecular adaptor activity 2 GO:0140657 ATP-dependent activity 1
Localization
GO:0005739 mitochondrion 3 GO:0005829 cytosol 1
Pathway
R-HSA-9612973 Autophagy 3 R-HSA-168256 Immune System 2 R-HSA-392499 Metabolism of proteins 2 R-HSA-8953854 Metabolism of RNA 2 R-HSA-5357801 Programmed Cell Death 1
Partners
ATG16L1ATG5BECN1FUNDC1MRG15NLRX1PINK1TOMM40
Complex memberships
NLRX1-TUFM-Atg5-Atg12-Atg16L1 autophagy complex

Evidence

Reading pass · 30 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1995 Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu (Thermus aquaticus ortholog), and GDPNP (GTP analog) at 2.7 Å resolution revealed that EF-Tu-GTP binds one side of the tRNA acceptor helix using all three domains, with binding sites for the aminoacylated CCA end and the phosphorylated 5' end at domain interfaces, and the T stem interacting with domain 3. The overall shape mimics EF-G-GDP, suggesting 'molecular mimicry' in the translational apparatus. X-ray crystallography (2.7 Å resolution) Science High 7491491
1992 Crystal structure of E. coli EF-Tu·GDP refined to 2.6 Å revealed a three-domain architecture: an α/β domain (residues 1–200) containing the GDP-binding site, and two antiparallel β-barrel domains. This defined the inactive GDP-bound conformation. X-ray crystallography (2.6 Å resolution) Journal of Molecular Biology High 1542116
1993 Crystal structure of Thermus aquaticus EF-Tu·GDPNP (GTP analog) at 2.5 Å showed that the GDP→GTP transition induces ~90° rotation of domain 1 relative to domains 2 and 3, exposing the aminoacyl-tRNA binding site in the cleft at domain interfaces. Active-site residues affected in tRNA binding localize to or near this cleft. X-ray crystallography (2.5 Å resolution), structural comparison with E. coli EF-Tu·GDP Structure High 8069622
1997 Crystal structure of EF-Tu·EF-Ts complex from Thermus thermophilus revealed that EF-Ts induces a peptide flip in the nucleotide-binding pocket that disrupts hydrogen bonds to GDP phosphates and sterically/electrostatically ejects GDP, defining the guanine nucleotide exchange mechanism. The complex is a dyad-symmetrical heterotetramer where each EF-Tu interacts with two EF-Ts subunits via a bipartite interface. X-ray crystallography (crystal structure of EF-Tu·EF-Ts complex) Nature Structural Biology High 9253415
2009 Crystal structure of the bacterial ribosome complexed with EF-Tu and aminoacyl-tRNA at 3.6 Å resolution revealed the tRNA distortion allowing simultaneous interaction with the 30S decoding center and EF-Tu at the factor binding site. A series of conformational changes in EF-Tu and aminoacyl-tRNA suggests a communication pathway between the decoding center and the GTPase center of EF-Tu for GTP hydrolysis upon codon recognition. X-ray crystallography (3.6 Å resolution, ribosome·EF-Tu·aa-tRNA complex) Science High 19833920
2000 Crystal structure of bovine mitochondrial TUFM·GDP at 1.94 Å resolution showed overall similarity to prokaryotic EF-Tu·GDP but with altered orientation of domain 1 relative to domains 2 and 3. Mitochondrial EF-Tu binds nucleotides less tightly than prokaryotic EF-Tu, possibly due to increased mobility near the GDP-binding site. The C-terminal extension has structural similarities to DNA-recognizing zinc fingers, suggesting involvement in RNA recognition. X-ray crystallography (1.94 Å resolution) Journal of Molecular Biology High 10715211
1996 Crystal structure of E. coli EF-Tu·GDP in complex with GE2270 A antibiotic at 2.5 Å showed that the Switch I region adopts an ordered β-strand conformation in the GDP form, representing an α-to-β secondary structure switch relative to the GTP form. This GTP→GDP α-to-β switch is proposed as a prototypical activation/inactivation mechanism. X-ray crystallography (2.5 Å resolution) Structure High 8939740
2001 Crystal structure of EF-Tu·GDP·aurodox (kirromycin-type antibiotic) at 2.0 Å showed that aurodox locks EF-Tu in a GTP-like conformation even when GDP is bound, explaining how it prevents EF-Tu release from the ribosome. The structure also revealed that His-85 reorients toward the nucleotide-binding site and may stabilize the GTP hydrolysis transition state. X-ray crystallography (2.0 Å resolution) Journal of Biological Chemistry High 11278992
1988 Chemical probing of E. coli ribosomes showed that EF-Tu produces footprints at positions 2,655 and 2,661 of the universally conserved loop (sarcin-ricin loop, SRL) in domain VI of 23S rRNA in vitro, identifying this rRNA region as a contact site for EF-Tu on the ribosome. Chemical footprinting (in vitro and in vivo) Nature Medium 2455872
2006 NMR spectroscopy demonstrated that ribosomal protein L12 directly binds to EF-Tu (and also IF2, EF-G, RF3) via a conserved region of the L12 C-terminal domain (involving residues K70, L80, E82). All four factors bind the same region, and binding causes broadening of all C-terminal domain signals while the N-terminal domain retains mobility. Heteronuclear NMR spectroscopy, chemical shift mapping Journal of Molecular Biology High 17070545
2012 TUFM (mitochondrial EF-Tu) was identified as a direct interacting partner of NLRX1 by quantitative mass spectrometry and endogenous co-immunoprecipitation. TUFM inhibits RLR-induced type I interferon production and promotes autophagy during viral infection. TUFM also interacts with the autophagy complex Atg5-Atg12 and Atg16L1. High-throughput quantitative mass spectrometry, endogenous co-immunoprecipitation, knockdown/knockout functional assays Immunity High 22749352
2013 TUFM interacts with Atg5-Atg12 and Atg16L1 to form a molecular complex that promotes autophagy and reduces RIG-I/DDX58-activated cytokine production. NLRX1 and TUFM work in concert via this complex. Co-immunoprecipitation, functional knockdown assays Autophagy Medium 23321557
2006 Mutations in TUFM (mitochondrial elongation factor Tu, EFTu) cause severe infantile lactic acidosis, progressive fatal encephalopathy, and macrocystic leukodystrophy with micropolygyria. Patient cells showed defective mitochondrial DNA translation, and yeast and mammalian cell complementation assays demonstrated the pathogenic role of mutant TUFM alleles in mitochondrial translation. Functional complementation in yeast and mammalian cells, structural modeling American Journal of Human Genetics High 17160893
2008 Overexpression of EFTu (but not EFTs or EFG1) partially suppressed the mitochondrial translation and respiratory chain assembly defects of MELAS A3243G mutant myoblasts, demonstrating that EFTu levels directly modulate mitochondrial translation fidelity and efficiency. Amino acid misincorporation was detected in CO III, CO II, and ATP6 in mutant cells. Blue-Native gel electrophoresis, pulse-chase labeling, endoproteinase fingerprint analysis, overexpression rescue Human Molecular Genetics High 18753147
2020 TUFM has a non-canonical dual-localization (mitochondria and cytosol) and regulates mitophagy via interaction with PINK1. PINK1-dependent phosphorylation of TUFm at Ser222 constitutes a phosphoswitch: unphosphorylated TUFm activates mitophagy, while p-S222-TUFm is restricted to the cytosol where it inhibits mitophagy by impeding Atg5-Atg12 formation. This Parkin-independent route is evolutionarily conserved. Co-immunoprecipitation, phosphosite mutagenesis (S222A/S222E), subcellular fractionation, live imaging, genetic epistasis, in vitro kinase assays Molecular Cell High 33113344
2021 TUFM localizes in part on the outer mitochondrial membrane (OMM) and inhibits caspase-8-mediated apoptosis through its autophagic/mitophagic function. The GxxxG motif within the N-terminal mitochondrial targeting sequences is required for TUFM self-dimerization on the OMM and for mitophagy. Autophagy-competent TUFM on the OMM is stabilized upon mitophagy activation and is subject to ubiquitin-proteasome degradation under basal conditions. Inducible knockdown, subcellular fractionation, apoptosis assays (caspase-8 activation), site-directed mutagenesis (GxxxG motif), co-immunoprecipitation Cell Death and Differentiation High 34511600
2021 Kaempferide (Kaem) directly interacts with TUFM as identified by drug affinity responsive target stability (DARTS) and LC-MS/MS. TUFM activates autophagy and lipid degradation via mitochondrial ROS (mtROS)-mediated lysosomal Ca2+ efflux and TFEB translocation (without MTOR perturbation). TUFM absence reversed Kaem-induced autophagy and lipid degradation. DARTS combined with LC-MS/MS target identification, TUFM knockdown, ROS measurement, lysosomal Ca2+ imaging, TFEB translocation assay, in vivo diet-induced obesity mouse model Communications Biology High 33398033
2016 TUFM serves as an anchorage site that recruits Beclin-1 to mitochondria, promotes its polyubiquitination, and interferes with Beclin-1's interaction with Rubicon, thereby promoting autophagic flux. The NLRX1-TUFM complex is required for autophagy induction in HNSCC cells treated with EGFR inhibitors. Co-immunoprecipitation, ubiquitination assays, TUFM knockdown, autophagic flux assays Oncogene Medium 26876213
2016 TUFM knockdown in A549 lung cancer cells induced epithelial-mesenchymal transition (EMT), reduced mitochondrial respiratory chain activity, increased ROS, activated AMPK, phosphorylated GSK3β, and increased nuclear β-catenin, demonstrating that TUFM suppresses the AMPK-GSK3β-β-catenin axis to maintain epithelial phenotype. siRNA knockdown, mitochondrial respiration assay, ROS measurement, immunoblotting (AMPK, GSK3β, β-catenin phosphorylation), migration assays Cellular and Molecular Life Sciences Medium 26781467
2022 MRG15 interacts with TUFM at the outer mitochondrial membrane and deacetylates TUFM at K82 and K91. Deacetylated TUFM undergoes accelerated degradation by the mitochondrial ClpXP protease system. Reduced TUFM results in impaired mitophagy, increased oxidative stress, and NLRP3 inflammasome activation in NASH. Co-immunoprecipitation-mass spectrometry, CRISPR gene depletion in vivo, acetylation site mutagenesis, ClpXP protease assay Journal of Hepatology High 35985547
2022 FUNDC1 interacts with TUFM via its 96–133 amino acid domain to maintain mitochondrial DNA stability and prevent cytoplasmic mtDNA release. TUFM knockdown reversed FUNDC1-mediated protection against DOX-induced mtDNA cytosolic release and PANoptosis. Co-immunoprecipitation with defined domain mapping, TUFM knockdown rescue experiments, mtDNA cytosolic release assay Cell Death and Disease Medium 36470869
2024 TUFM lactylation at K286 inhibits its interaction with TOMM40 on mitochondria, restricting mitochondrial distribution of TUFM and suppressing TUFM-mediated mitophagy, thereby increasing neuronal apoptosis after traumatic brain injury. A lactylation-deficient TUFmK286R knockin rescued mitochondrial TUFM distribution, mitophagy, and functional outcomes after cortical impact. Lactylation mass spectrometry screen, site-specific knockin (K286R), co-immunoprecipitation, mitophagy assays, in vivo mouse cortical impact model Cell Death and Differentiation High 39496783
2024 SFTSV nucleoprotein (NP) translocates to mitochondria by interacting with TUFM, and mediates mitophagy via LC3 interaction (requiring the NP N-terminal LIR motif), leading to MAVS degradation and evasion of antiviral innate immunity. Co-immunoprecipitation, subcellular fractionation, LC3-interaction mutagenesis, mitophagy assays, innate immune signaling assays Autophagy Medium 39189526
2024 SVA 2C protein directly interacts with TUFM at glutamic acids E196 and E211. E3 ubiquitin ligase RNF185 catalyzes K27-linked polyubiquitination of TUFM through interaction of RNF185's transmembrane domain 1 with TUFM. K27-ubiquitinated TUFM is then recognized by SQSTM1/p62, which recruits LC3, linking mitochondria to phagophores to induce mitophagy that promotes SVA replication. Co-immunoprecipitation, site-directed mutagenesis (E196/E211), ubiquitination assays, K27 linkage-specific analysis, genome-wide SVA protein screen Autophagy High 38084826
2017 TUFM shows higher binding affinity for avian-signature PB2627E of influenza A virus than for human-signature PB2627K as determined by immunoprecipitation and differential proteomics. TUFM overexpression specifically inhibits PB2627E virus replication while TUFM deficiency increases PB2627E replication; TUFM-dependent autophagy correlates with this restriction. Co-immunoprecipitation, differential proteomics, TUFM knockdown/overexpression, viral replication assays, mitochondrial fractionation mBio Medium 28611246
1997 The human mitochondrial TUFM gene was cloned; the encoded protein is ~49.8 kDa with a ~50-aa N-terminal mitochondrial leader sequence, and shows high similarity to bacterial and yeast EF-Tu. The gene spans ~3.6 kb with nine introns and maps to chromosome 16p11.2. A pseudogene (92.6% identity) was mapped to 17q11.2. cDNA cloning, Northern blot, genomic sequencing, chromosomal mapping by FISH Gene Medium 9332382
1998 E. coli EF-Tu has chaperone-like activity: it promotes refolding of citrate synthase and α-glucosidase after urea denaturation, prevents aggregation of citrate synthase under heat shock, and forms stable complexes with unfolded proteins. EF-Tu·GDP is substantially more active than EF-Tu·GTP in stimulating protein renaturation. EF-Tu binds hydrophobic regions of substrate proteins. In vitro renaturation assay, co-sedimentation/complex formation assay, nucleotide-specific activity comparison Journal of Biological Chemistry Medium 9565560
2013 Doc, a Fic-family toxin-antitoxin protein, inhibits bacterial translation by phosphorylating the conserved Thr382 of EF-Tu, rendering EF-Tu unable to bind aminoacylated tRNAs. Doc uses antiparallel NTP binding relative to canonical Fic catalytic residues, establishing a new type of kinase activity evolved from AMPylation. In vitro kinase assay, site-directed mutagenesis, aminoacyl-tRNA binding assay, structural modeling Nature Chemical Biology High 24141193
1997 The yeast mitochondrial Ef-Tu (TUF M) gene dosage on a multicopy plasmid can suppress heat-sensitive growth defects caused by a mutation affecting 3'-end processing of mitochondrial tRNAAsp, suggesting that elevated TUFM can compensate for defects in mitochondrial tRNA maturation. Genetic suppression screen (multicopy suppressor), temperature-sensitive growth complementation Current Genetics Medium 9211792
2021 TUFM knockdown or overexpression in HEK-APP cells increases or decreases BACE1 protein and mRNA levels, respectively, through a ROS-dependent mechanism affecting BACE1 mRNA stability (not transcription). TUFM-mediated regulation of apoptosis and Tau phosphorylation was also attenuated by mitochondria-targeted antioxidant, indicating that TUFM controls these pathologies via mitochondrial ROS. siRNA knockdown, overexpression, mRNA stability assay (actinomycin D chase), ROS measurement, mitochondria-targeted antioxidant treatment FASEB Journal Medium 33774866

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation. Cell 1355 16713565
1995 Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Science (New York, N.Y.) 779 7491491
1988 Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNA. Nature 441 2455872
2009 The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA. Science (New York, N.Y.) 402 19833920
1993 The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure (London, England : 1993) 360 8069622
2012 The mitochondrial proteins NLRX1 and TUFM form a complex that regulates type I interferon and autophagy. Immunity 262 22749352
1992 Refined structure of elongation factor EF-Tu from Escherichia coli. Journal of molecular biology 257 1542116
1998 Chaperone properties of bacterial elongation factor EF-Tu. The Journal of biological chemistry 207 9565560
2021 Activation of mitochondrial TUFM ameliorates metabolic dysregulation through coordinating autophagy induction. Communications biology 192 33398033
1996 An alpha to beta conformational switch in EF-Tu. Structure (London, England : 1993) 176 8939740
2006 Infantile encephalopathy and defective mitochondrial DNA translation in patients with mutations of mitochondrial elongation factors EFG1 and EFTu. American journal of human genetics 162 17160893
2019 The Diverse Functional Roles of Elongation Factor Tu (EF-Tu) in Microbial Pathogenesis. Frontiers in microbiology 152 31708880
2013 The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu. Nature chemical biology 148 24141193
1994 Protein synthesis elongation factor EF-1 alpha is essential for ubiquitin-dependent degradation of certain N alpha-acetylated proteins and may be substituted for by the bacterial elongation factor EF-Tu. Proceedings of the National Academy of Sciences of the United States of America 143 8052636
2022 FUNDC1 protects against doxorubicin-induced cardiomyocyte PANoptosis through stabilizing mtDNA via interaction with TUFM. Cell death & disease 126 36470869
2008 The A3243G tRNALeu(UUR) MELAS mutation causes amino acid misincorporation and a combined respiratory chain assembly defect partially suppressed by overexpression of EFTu and EFG2. Human molecular genetics 118 18753147
1997 Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus. Nature structural biology 118 9253415
2006 The ribosomal stalk binds to translation factors IF2, EF-Tu, EF-G and RF3 via a conserved region of the L12 C-terminal domain. Journal of molecular biology 106 17070545
2001 Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox. The Journal of biological chemistry 104 11278992
2002 The tRNA specificity of Thermus thermophilus EF-Tu. Proceedings of the National Academy of Sciences of the United States of America 96 11891293
2010 Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein. Proceedings of the National Academy of Sciences of the United States of America 91 20133608
2009 Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-Tu. Quarterly reviews of biophysics 85 20025795
2013 The NLR protein, NLRX1, and its partner, TUFM, reduce type I interferon, and enhance autophagy. Autophagy 73 23321557
1985 Mutants of the elongation factor EF-Tu, a new class of nonsense suppressors. The EMBO journal 73 3926487
2007 Expression of the mucus adhesion genes Mub and MapA, adhesion-like factor EF-Tu and bacteriocin gene plaA of Lactobacillus plantarum 423, monitored with real-time PCR. International journal of food microbiology 71 17399831
1997 Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF-Tu flexing. The Journal of biological chemistry 63 9405422
1999 Quantitative assessment of EF-1alpha.GTP binding to aminoacyl-tRNAs, aminoacyl-viral RNA, and tRNA shows close correspondence to the RNA binding properties of EF-Tu. The Journal of biological chemistry 61 9873000
1994 The structural and functional basis for the kirromycin resistance of mutant EF-Tu species in Escherichia coli. The EMBO journal 59 7525272
2016 EGFR-targeted mAb therapy modulates autophagy in head and neck squamous cell carcinoma through NLRX1-TUFM protein complex. Oncogene 57 26876213
2009 CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis. Microbiology (Reading, England) 56 19246764
1986 Mutant EF-Tu increases missense error in vitro. Molecular & general genetics : MGG 56 3540529
2020 Paradoxical Mitophagy Regulation by PINK1 and TUFm. Molecular cell 55 33113344
2012 Association of Acinetobacter baumannii EF-Tu with cell surface, outer membrane vesicles, and fibronectin. TheScientificWorldJournal 55 22666090
2000 High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP. Journal of molecular biology 55 10715211
1983 The role of EF-Tu in the expression of tufA and tufB genes. European journal of biochemistry 54 6337847
2016 TUFM downregulation induces epithelial-mesenchymal transition and invasion in lung cancer cells via a mechanism involving AMPK-GSK3β signaling. Cellular and molecular life sciences : CMLS 53 26781467
1994 Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu.GTP. FEBS letters 53 7925958
2015 A synthetic tRNA for EF-Tu mediated selenocysteine incorporation in vivo and in vitro. FEBS letters 51 26160755
1976 Elongation factor T from Bacillus stearothermophilus and Escherichia coli. Purification and some properties of EF-Tu and EF-Ts from Bacillus stearothermophilus. European journal of biochemistry 51 767105
2002 Mechanisms of EF-Tu, a pioneer GTPase. Progress in nucleic acid research and molecular biology 50 12102560
2018 Elongation Factor Thermo Unstable (EF-Tu) Moonlights as an Adhesin on the Surface of Mycoplasma hyopneumoniae by Binding to Fibronectin. Frontiers in microbiology 49 29867877
2017 Inhibition of Avian Influenza A Virus Replication in Human Cells by Host Restriction Factor TUFM Is Correlated with Autophagy. mBio 49 28611246
2010 Assembly of Q{beta} viral RNA polymerase with host translational elongation factors EF-Tu and -Ts. Proceedings of the National Academy of Sciences of the United States of America 49 20798060
2013 Lysine trimethylation of EF-Tu mimics platelet-activating factor to initiate Pseudomonas aeruginosa pneumonia. mBio 48 23653444
2010 Cleavage of the sarcin-ricin loop of 23S rRNA differentially affects EF-G and EF-Tu binding. Nucleic acids research 47 20215430
1988 Mutations in ribosomal proteins L7/L12 perturb EF-G and EF-Tu functions. Biochimie 47 3139080
2003 EF-Tu binding peptides identified, dissected, and affinity optimized by phage display. Chemistry & biology 46 12618188
1977 Conformational alteration of protein synthesis elongation factor EF-Tu by EF-Ts and by kirromycin. Proceedings of the National Academy of Sciences of the United States of America 46 269389
2021 Autophagy-competent mitochondrial translation elongation factor TUFM inhibits caspase-8-mediated apoptosis. Cell death and differentiation 45 34511600
1994 Synergism between the GTPase activities of EF-Tu.GTP and EF-G.GTP on empty ribosomes. Elongation factors as stimulators of the ribosomal oscillation between two conformations. Journal of molecular biology 44 7932721
2024 Tufm lactylation regulates neuronal apoptosis by modulating mitophagy in traumatic brain injury. Cell death and differentiation 43 39496783
2018 Oxidation of Translation Factor EF-Tu Inhibits the Repair of Photosystem II. Plant physiology 43 29439212
2013 The expression of adhesin EF-Tu in response to mucin and its role in Lactobacillus adhesion and competitive inhibition of enteropathogens to mucin. Journal of applied microbiology 43 23663754
1989 Genes for the ribosomal proteins S12 and S7 and elongation factors EF-G and EF-Tu of the cyanobacterium, Anacystis nidulans: structural homology between 16S rRNA and S7 mRNA. Molecular & general genetics : MGG 43 2499762
2001 Identification of thermodynamically relevant interactions between EF-Tu and backbone elements of tRNA. Journal of molecular biology 40 11352580
1984 Specific alterations of the EF-Tu polypeptide chain considered in the light of its three-dimensional structure. The EMBO journal 40 6323160
2022 MRG15 aggravates non-alcoholic steatohepatitis progression by regulating the mitochondrial proteolytic degradation of TUFM. Journal of hepatology 38 35985547
2020 Anti-vimentin, anti-TUFM, anti-NAP1L1 and anti-DPYSL2 nanobodies display cytotoxic effect and reduce glioblastoma cell migration. Therapeutic advances in medical oncology 38 32426045
1998 Protein-disulfide isomerase activity of elongation factor EF-Tu. Biochemical and biophysical research communications 38 9813162
1990 Both genes for EF-Tu in Salmonella typhimurium are individually dispensable for growth. Journal of molecular biology 37 2168947
2007 The 51-63 base pair of tRNA confers specificity for binding by EF-Tu. RNA (New York, N.Y.) 35 17449728
1993 Growth and translation elongation rate are sensitive to the concentration of EF-Tu. Molecular microbiology 34 8332067
2019 Light-inducible expression of translation factor EF-Tu during acclimation to strong light enhances the repair of photosystem II. Proceedings of the National Academy of Sciences of the United States of America 33 31570574
1997 The human mitochondrial elongation factor tu (EF-Tu) gene: cDNA sequence, genomic localization, genomic structure, and identification of a pseudogene. Gene 33 9332382
1997 The ternary complex of EF-Tu and its role in protein biosynthesis. Current opinion in structural biology 31 9032056
1982 The structure of the EF-Tu . GDP . Me2+ complex. European journal of biochemistry 30 7200884
1976 Function and structure in ribonucleic acid phage Qbeta ribonucleic acid replicase. Effect of inhibitors of EF-Tu on ribonucleic acid synthesis and renaturation of active enzyme. The Journal of biological chemistry 30 1262342
1976 Renaturation of a multisubunit multiactivity enzyme complex: recovery of phage Qbeta RNA replicase, EF-Tu, and EF-Ts activities after denaturation in urea. Biochemistry 30 764866
1984 Histidine residues in elongation factor EF-tu from Escherichia coli protected by aminoacyl-tRNA against photo-oxidation. European journal of biochemistry 29 6386466
1996 An elongation factor Tu (EF-Tu) resistant to the EF-Tu inhibitor GE2270 in the producing organism Planobispora rosea. Molecular microbiology 28 8899707
2009 Heat tolerance and expression of protein synthesis elongation factors, EF-Tu and EF-1α, in spring wheat. Functional plant biology : FPB 27 32688642
1999 The characterization of Mycoplasma synoviae EF-Tu protein and proteins involved in hemadherence and their N-terminal amino acid sequences. FEMS microbiology letters 27 10220885
1997 Additional copies of the mitochondrial Ef-Tu and aspartyl-tRNA synthetase genes can compensate for a mutation affecting the maturation of the mitochondrial tRNAAsp. Current genetics 27 9211792
2006 Functional Qbeta replicase genetically fusing essential subunits EF-Ts and EF-Tu with beta-subunit. Journal of bioscience and bioengineering 26 16781472
1989 Comparison of the computed structures for the phosphate-binding loop of the p21 protein containing the oncogenic site Gly 12 with the X-ray crystallographic structures for this region in the p21 protein and EFtu. A model for the structure of the p21 protein in its oncogenic form. Journal of biomolecular structure & dynamics 26 2686707
2024 Senecavirus A induces mitophagy to promote self-replication through direct interaction of 2C protein with K27-linked ubiquitinated TUFM catalyzed by RNF185. Autophagy 25 38084826
2021 TUFM is involved in Alzheimer's disease-like pathologies that are associated with ROS. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 25 33774866
2007 Identification of Mycobacterium using the EF-Tu encoding (tuf) gene and the tmRNA encoding (ssrA) gene. Journal of medical microbiology 25 17644709
1988 The elongation factor EF-Tu from E. coli binds to the upstream activator region of the tRNA-tufB operon. Nucleic acids research 25 3057439
2019 A novel TUFM homozygous variant in a child with mitochondrial cardiomyopathy expands the phenotype of combined oxidative phosphorylation deficiency 4. Journal of human genetics 24 30903008
2011 Identification and cloning of two immunogenic Clostridium perfringens proteins, elongation factor Tu (EF-Tu) and pyruvate:ferredoxin oxidoreductase (PFO) of C. perfringens. Research in veterinary science 24 21345474
1995 Antibiotic resistance mechanisms of mutant EF-Tu species in Escherichia coli. Biochemistry and cell biology = Biochimie et biologie cellulaire 24 8722034
1994 Why do two EF-Tu molecules act in the elongation cycle of protein biosynthesis? Trends in biochemical sciences 24 8048158
2015 EF-Tu dynamics during pre-translocation complex formation: EF-Tu·GDP exits the ribosome via two different pathways. Nucleic acids research 23 26338772
1997 An A to U transversion at position 1067 of 23 S rRNA from Escherichia coli impairs EF-Tu and EF-G function. Journal of molecular biology 23 9325093
1996 Identification of an EF-Tu protein that is periplasm-associated and processed in Neisseria gonorrhoeae. Microbiology (Reading, England) 23 8828215
2024 Bunyavirus SFTSV nucleoprotein exploits TUFM-mediated mitophagy to impair antiviral innate immunity. Autophagy 22 39189526
2017 Novel mutation in mitochondrial Elongation Factor EF-Tu associated to dysplastic leukoencephalopathy and defective mitochondrial DNA translation. Biochimica et biophysica acta. Molecular basis of disease 22 28132884
2013 An unusual mechanism for EF-Tu activation during tmRNA-mediated ribosome rescue. RNA (New York, N.Y.) 22 24345396
2011 Is the sequence-specific binding of aminoacyl-tRNAs by EF-Tu universal among bacteria? Nucleic acids research 22 21893586
2010 Identification of Rack1, EF-Tu and Rhodanese as aging-related proteins in human colonic epithelium by proteomic analysis. Journal of proteome research 22 20099848
2008 A signal relay between ribosomal protein S12 and elongation factor EF-Tu during decoding of mRNA. RNA (New York, N.Y.) 22 19095621
2000 The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability. Journal of biochemical and biophysical methods 22 10647810
1991 Error-prone EF-Tu reduces in vivo enzyme activity and cellular growth rate. Molecular microbiology 22 1710757
1984 Modification of amino groups in EF-Tu.GTP and the ternary complex EF-Tu.GTP.valyl-tRNAVal. European journal of biochemistry 22 6430701
2015 Borrelia burgdorferi elongation factor EF-Tu is an immunogenic protein during Lyme borreliosis. Emerging microbes & infections 21 26954993
2002 Specificity of elongation factor EF-TU for hydrophobic peptides. Biochemical and biophysical research communications 21 12176046
1992 Sequence of the tufA gene encoding elongation factor EF-Tu from Thermus aquaticus and overproduction of the protein in Escherichia coli. European journal of biochemistry 21 1499561
2022 Silencing TUFM Inhibits Development of Monocrotaline-Induced Pulmonary Hypertension by Regulating Mitochondrial Autophagy via AMPK/mTOR Signal Pathway. Oxidative medicine and cellular longevity 20 35936222
2018 Glioblastoma-specific anti-TUFM nanobody for in-vitro immunoimaging and cancer stem cell targeting. Oncotarget 20 29707108

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