Affinage

H3C15

Histone H3.2 · UniProt Q71DI3

Length
136 aa
Mass
15.4 kDa
Annotated
2026-06-10
28 papers in source corpus 23 papers cited in narrative 23 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

H3C15 encodes a canonical histone H3 whose N-terminal tail functions as a multifunctional regulatory platform controlling chromatin compaction, transcriptional repression, and differentiation (PMID:15280228, PMID:19666585). In yeast, the H3 N-terminus represses GAL-regulated genes and demarcates euchromatin from heterochromatin: its lysines K4, K9, K14, K18, K23 and K27 act redundantly to maintain subtelomeric silencing (PMID:1505519, PMID:15280228), and the tail is dispensable for Sir protein recruitment but required to assemble the higher-order silent chromatin structure that follows (PMID:19666585). The tail's accessibility within the nucleosome is structurally constrained — it is clamped between DNA gyres in the core particle, repositions onto linker DNA in the chromatosome, and follows DNA motions in solution while allosterically sensing core charge changes (PMID:31956896, PMID:35265811) — and these dynamics are actively remodeled by the FACT complex, which asymmetrically exposes one tail during nucleosome unwrapping (PMID:33103079). Beyond reversible PTMs, the tail is subject to irreversible proteolytic clipping by an array of nuclear proteases that removes activation-associated marks and licenses transcriptional activation during differentiation and in cancer: MMP-2 cleaves between K18 and Q19 at the +1 nucleosome of active genes to drive myogenesis and activate the secondary protease CTSB (PMID:34001241, PMID:37161413), MMP-9 clips the tail during osteoclast differentiation and to activate growth genes in colon cancer (PMID:30992059, PMID:38600695), HDAC1 has intrinsic protease activity cleaving between K20 and A21 in bladder cancer (PMID:41286098), JMJD5 cleaves at monomethyl-lysine under DNA damage stress (PMID:28982940), and yeast Prb1 cleaves between K23 and A24 (PMID:24587380); dCas9-tethering of MMP-9 or HDAC1 establishes that proteolysis per se is the causal epigenetic switch (PMID:38600695, PMID:41286098). The tail also serves as a docking site for effectors including the H1 C-terminal domain (PMID:33125082), PHD-finger proteins such as PHRF1 (whose H3-binding is required for the DNA damage response) and PHF2 (PMID:33969871, PMID:40671529), and T-box transcription factors (PMID:17630961). Cancer-associated arginine mutations (H3R2C, H3R26C) disrupt PRC2-mediated H3K27me3 domains, de-repressing differentiation programs (PMID:38886411).

Mechanistic history

Synthesis pass · year-by-year structured walk · 23 steps
  1. 1992 High

    Established that the H3 N-terminal tail, distinct from the H4 tail, is required for transcriptional repression, defining a regulatory function for the tail beyond structural packaging.

    Evidence Deletion and acetylation-site substitution mutants with GAL reporter readouts in yeast

    PMID:1505519

    Open questions at the time
    • Did not identify the effector proteins reading the tail
    • Limited to GAL-regulated promoters
  2. 2004 High

    Showed the H3 tail lysines act redundantly to demarcate euchromatin from heterochromatin, explaining why single-site mutations had failed to reveal a silencing role.

    Evidence Systematic N-terminal tail mutagenesis with genome-wide expression analysis in S. cerevisiae

    PMID:15280228

    Open questions at the time
    • Mechanism of redundancy unresolved
    • Did not distinguish PTM-dependent vs PTM-independent contributions
  3. 2009 High

    Resolved where the H3 tail acts in the silencing pathway, showing it is dispensable for Sir recruitment but required to form higher-order compacted chromatin downstream.

    Evidence Genome-wide ChIP, dam methylase accessibility, and sucrose gradient fractionation in yeast

    PMID:19666585

    Open questions at the time
    • Molecular nature of the higher-order structure not defined
    • No structural model of compaction
  4. 2007 Medium

    Identified T-box transcription factors as H3 tail-interacting proteins, linking the tail to mitotic chromatin recognition.

    Evidence Pulldown, in vitro nucleosome binding, imaging, and ectopic expression with mitotic phenotype readout

    PMID:17630961

    Open questions at the time
    • Binding interface on the tail not mapped
    • Functional consequence of the interaction in vivo limited
  5. 2011 Medium

    Defined how arginine and lysine modifications across the tail gate H3 kinase activity, linking tail PTM state to mitotic phosphorylation.

    Evidence In vitro kinase assays with defined-modification H3 peptides (AURKB, Haspin)

    PMID:21397507

    Open questions at the time
    • No cellular validation
    • Peptide substrates may not reflect nucleosomal context
  6. 2014 High

    Identified yeast Prb1 as the principal H3 tail protease and mapped its cleavage site, establishing proteolytic clipping as a regulated tail modification in yeast.

    Evidence Biochemical fractionation, in vitro cleavage with purified Prb1, Edman degradation, PRB1 deletion

    PMID:24587380

    Open questions at the time
    • Physiological trigger for clipping unclear
    • Downstream transcriptional consequences not defined
  7. 2014 Medium

    Linked H3 tail PTMs to chromatin remodeler regulation, showing modified tails control RUVBL1/2 ATPase activity and oligomeric state.

    Evidence Pulldown, ATPase assays with modified H3 peptides, oligomerization analysis, ChIP at progesterone receptor promoter

    PMID:25336637

    Open questions at the time
    • Direct structural basis of tail-Reptin/Pontin contact not resolved
    • In vivo significance of oligomer switch limited
  8. 2016 Medium

    Connected a specific tail lysine (K14) to rDNA silencing via CAF-1-dependent nucleosome assembly rather than RENT recruitment.

    Evidence Yeast mutagenesis, silencing assays, RENT ChIP, CAF-1 analysis, replicative aging assay

    PMID:26906758

    Open questions at the time
    • Mechanism linking K14 to Cac2 levels unresolved
    • Single residue; broader tail context not tested
  9. 2017 High

    Characterized JMJD5 as a Kme1-specific H3 tail protease acting at repressed promoters under DNA damage, extending the protease repertoire to methyl-mark readers.

    Evidence In vitro peptide digestion and in vivo stress-induced cleavage assays

    PMID:28982940

    Open questions at the time
    • Genome-wide cleavage targets not mapped
    • Functional outcome of K9 clipping not defined
  10. 2019 Medium

    Showed PTM state directs protease access, with H3K18ac/K27me1 facilitating MMP-9 cleavage during osteoclast differentiation.

    Evidence Pharmacological DNMT/HDAC inhibition, ChIP, qPCR, osteoclast differentiation and H3 cleavage assays

    PMID:30992059

    Open questions at the time
    • Direct MMP-9 cleavage site on H3 not defined here
    • Reliance on pharmacological inhibitors
  11. 2020 Medium

    Established that the H3 tail directly interacts with the H1 C-terminal domain to regulate chromatin condensation through protein-protein contact rather than DNA geometry.

    Evidence FRET condensation measurements with H3 tail deletion and acetylation-mimic constructs on reconstituted nucleosomes

    PMID:33125082

    Open questions at the time
    • Tail-H1 interface residues not mapped
    • Single reconstituted system
  12. 2020 Medium

    Defined the constrained dynamics of the tail, showing it tracks DNA motion and allosterically senses core charge changes coupled to DNA unwrapping.

    Evidence High-precision single-molecule FRET on reconstituted mononucleosomes

    PMID:31956896

    Open questions at the time
    • In vivo relevance of dynamic modes untested
    • Allosteric pathway through the core not structurally resolved
  13. 2020 High

    Demonstrated FACT actively remodels tail accessibility, asymmetrically exposing one H3 tail during nucleosome unwrapping to bias acetylation.

    Evidence Cryo-EM of FACT-nucleosome intermediate plus NMR real-time acetylation monitoring

    PMID:33103079

    Open questions at the time
    • Functional consequence of asymmetry in vivo unknown
    • Whether asymmetry persists across remodeling cycles unclear
  14. 2021 High

    Identified MMP-2 as the principal H3 tail protease in myogenesis, mapping the K18/Q19 cleavage site and showing nuclear (not ECM) MMP-2 drives differentiation.

    Evidence Zymography, RNAi, ECM supplementation, cleavage assays, myogenic differentiation

    PMID:34001241

    Open questions at the time
    • How MMP-2 enters/targets the nucleus not defined
    • Genome-wide cleavage sites addressed only later
  15. 2021 High

    Defined the conserved PHD-finger recognition code for the H3 tail (Met removal, R2 groove, K4me aromatic cage) and revealed non-histone H3 tail mimics competing for these readers.

    Evidence Domain microarray screen, crystal structure of PHF2 PHD-VRK1 K4me3, binding affinity measurements

    PMID:33969871

    Open questions at the time
    • Cellular impact of H3TM competition not established
    • Scope of mimicry across the proteome incomplete
  16. 2021 High

    Provided in vivo evidence that H3 tail clipping by Trypsins and Cathepsin L accompanies intestinal epithelial differentiation, with PTM state tuning protease activity.

    Evidence Biochemical fractionation, 3D organoids, mouse intestinal tissue, protease identification

    PMID:33398338

    Open questions at the time
    • Direct causal link between clipping and gene activation in vivo not isolated
    • Cleavage sites for each protease not all mapped
  17. 2022 High

    Resolved how nucleosomal context governs tail accessibility, showing the tail is clamped between DNA gyres in the core particle but repositions onto linker DNA in the chromatosome, with H4 tail acetylation enhancing H3 tail acetylation.

    Evidence NMR of H3 tail dynamics and acetylation across NCP, nucleosome, and chromatosome particles

    PMID:35265811

    Open questions at the time
    • In vivo chromatosome state not directly probed
    • Coupling to higher-order folding not addressed
  18. 2023 High

    Mapped MMP-2 H3 tail proteolysis genome-wide to +1 nucleosomes of active genes, coupling clipping to loss of activating PTMs and activation of secondary protease CTSB.

    Evidence ChIP-seq for MMP-2 localization, cleavage assays, PTM ChIP-qPCR

    PMID:37161413

    Open questions at the time
    • Recruitment mechanism of MMP-2 to TSSs unclear
    • Hierarchy of MMP-2 vs CTSB action not fully ordered
  19. 2024 High

    Provided direct causal evidence that H3 tail proteolysis itself drives oncogenic transcription, using dCas9-MMP-9 tethering to install transcriptional competence.

    Evidence MMP-9 knockdown/inhibition, ChIPac-qPCR, dCas9-MMP-9 targeting, transcriptomics, xenografts

    PMID:38600695

    Open questions at the time
    • How clipping is read by downstream machinery not defined
    • Reversibility / replacement of clipped H3 unclear
  20. 2024 High

    Showed cancer-associated tail arginine mutations (H3R2C, H3R26C) act in trans to disrupt PRC2-mediated H3K27me3 domains and impair differentiation.

    Evidence Cell-based mutant expression, H3K27me3 ChIP-seq, teratoma differentiation assays, cancer mutation analysis

    PMID:38886411

    Open questions at the time
    • Mechanism of trans-domain disruption not fully resolved
    • Tumor-type specificity not addressed
  21. 2025 High

    Established that PHRF1 PHD-finger binding to the H3 tail is required for the DNA damage response, with a cancer-associated P221L mutation abolishing both binding and rescue.

    Evidence Binding assays, PHD mutagenesis, PHRF1 knockout complementation, RNA-seq/proteomics, DDR assays

    PMID:40671529

    Open questions at the time
    • Which H3 tail PTM state PHRF1 prefers not fully defined
    • Downstream DDR effectors recruited by PHRF1 unclear
  22. 2025 High

    Revealed HDAC1 has intrinsic H3 tail protease activity (K20/A21 cleavage) required for oncogenic transcription, expanding the protease repertoire to a known deacetylase.

    Evidence In vitro and cellular cleavage assays, HDAC1 knockdown, dCas9-HDAC1 tethering, proliferation assays

    PMID:41286098

    Open questions at the time
    • Relationship between HDAC1 deacetylase and protease activities unresolved
    • Structural basis of protease activity not defined
  23. 2025 Medium

    Linked H3 threonine 3 phosphorylation to meiotic division and spindle-checkpoint surveillance in yeast.

    Evidence Yeast mutagenesis (T3A, K4A, S10A), sporulation/spore viability, MAD2 deletion epistasis

    PMID:40867646

    Open questions at the time
    • No molecular mechanism for how H3T3ph acts in meiosis
    • Effector reading H3T3ph not identified

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the diverse H3 tail proteases are recruited to specific loci, and how clipped H3 products are read, replaced, or recycled to propagate transcriptional outcomes, remains unresolved.
  • No unified model of protease targeting specificity
  • Fate of clipped nucleosomes (turnover vs retention) undefined
  • Reader proteins for clipped H3 not identified

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 4 GO:0140110 transcription regulator activity 4
Localization
GO:0000228 nuclear chromosome 3 GO:0005634 nucleus 3
Pathway
R-HSA-4839726 Chromatin organization 4 R-HSA-1266738 Developmental Biology 3 R-HSA-74160 Gene expression (Transcription) 3 R-HSA-73894 DNA Repair 2
Partners
H1.4HDAC1JMJD5MMP-2MMP-9PHF2PHRF1RUVBL2
Complex memberships
chromatosomenucleosome

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1992 Deletions of residues 4-15 and acetylation-site substitutions at residues 9, 14, and 18 within the histone H3 N-terminal tail allow hyperactivation of the GAL1 promoter and other GAL4-regulated genes in yeast, establishing that the H3 N-terminus functions in repression of GAL gene expression distinct from the H4 N-terminus role. In vivo genetic mutagenesis (deletion and substitution mutants) with reporter gene expression analysis in yeast The EMBO journal High 1505519
2004 The histone H3 N-terminal domain (not H4 N-terminal domain) is required for subtelomeric gene repression in yeast; mutating H3 lysine residues K4, K9, K14, K18, K23, and K27 collectively (but not individually) disrupts subtelomeric repression, indicating these lysines act redundantly to demarcate euchromatin from heterochromatin. Systematic N-terminal tail mutagenesis combined with genome-wide expression analysis in Saccharomyces cerevisiae Genetics High 15280228
2009 The H3 N-terminal tail is not required for Sir protein recruitment or spreading at telomeres and HM loci in yeast; instead, deletion of the H3 tail leads to increased chromatin accessibility (by dam methylase assay) and decreased mobility of heterochromatic fragments in sucrose gradients, indicating the H3 N-terminus is required for formation of higher-order silent chromatin structure after Sir proteins are recruited by the H4 tail. Genome-wide ChIP binding maps, ectopic dam methylase accessibility assay, sucrose gradient fractionation in yeast Proceedings of the National Academy of Sciences of the United States of America High 19666585
2017 JMJD5, a JmjC domain-containing protein, acts as a Cathepsin L-type protease that cleaves the histone H3 N-terminal tail exclusively at monomethyl-lysine (Kme1) residues in vitro; in vivo, K9 of H3 is the major cleavage site and H3.3 is the primary H3 target, with cleavage occurring under DNA damage stress at gene promoters repressed by JMJD5. In vitro H3 peptide digestion assay, in vivo protease activity under stress conditions, site-specific cleavage analysis EMBO reports High 28982940
2014 The yeast vacuolar protease Prb1 is the principal protease responsible for clipping the histone H3 N-terminal tail in Saccharomyces cerevisiae; purified Prb1 cleaves H3 between Lys23 and Ala24 in vitro, and endopeptidase activity is lost in prb1Δ mutants. Biochemical fractionation, in vitro cleavage assay with purified Prb1, Edman degradation to identify cleavage site, PRB1 deletion mutant analysis PloS one High 24587380
2007 T-box transcription factors (Tbx2, Tbx4, Tbx5, Tbx6) interact specifically with the histone H3 N-terminal tail; Tbx2 can recognize mitotic chromatin in a DNA-dependent manner and bind nucleosomal DNA, with nucleosome binding antagonized by the presence of histone tails; ectopic Tbx2 expression leads to mitotic defects. Pulldown/binding assays, in vitro nucleosome binding, co-localization by imaging, ectopic expression with mitotic phenotype readout Pigment cell research Medium 17630961
2011 Aurora kinase B (AURKB) activity toward H3 is affected by modifications spanning R2 to K14, while Haspin kinase activity is significantly affected by modifications at R2 and K4; dimethylation at R2 and R8 abolishes AURKB-promoted phosphorylation at S10, and dimethylation at R2 abolishes Haspin-promoted phosphorylation at T3. In vitro kinase activity assays using histone H3 N-terminal peptides with defined modifications Bioorganic & medicinal chemistry Medium 21397507
2014 Reptin/RUVBL2 and Pontin/RUVBL1 form stable complexes with nucleosomes, and their ATPase activity is modulated by acetylation and methylation of the histone H3 N-terminus; H3 tail peptides regulate the monomer-oligomer transition of Reptin/Pontin, with different oligomeric states pulling down distinct protein cofactors. Biochemical pulldown, ATPase activity assays with modified H3 peptides, monomer-oligomer transition analysis, in vivo ChIP at progesterone receptor gene promoter The Journal of biological chemistry Medium 25336637
2016 Mutation of histone H3 K14 (H3K14R) specifically disrupts rDNA silencing without affecting the RENT complex recruitment to rDNA; instead, K14R mutation reduces the level of CAF-1 subunit Cac2 and delays replication-dependent nucleosome assembly, advancing replicative lifespan. Genetic mutagenesis in yeast, silencing assays, ChIP for RENT complex, CAF-1 level analysis, replicative aging assay Scientific reports Medium 26906758
2019 MMP-9-dependent proteolysis of the histone H3 N-terminal tail during osteoclast differentiation is facilitated by H3K18 acetylation and H3K27 monomethylation; DNMT inhibition increases MMP-9 expression and H3NT proteolysis, while HDAC inhibition with TSA increases H3K27ac and reduces H3K27me1, impairing MMP-9-nucleosome interaction and H3NT proteolysis. Pharmacological inhibitor treatments, ChIP, qPCR, osteoclast differentiation assays, H3 cleavage biochemical assays Epigenetics & chromatin Medium 30992059
2020 The H3 N-terminal tail physically interacts directly with the intrinsically disordered H1 C-terminal domain (CTD); deletion of the H3 N-tail or installation of acetylation mimics within it alters condensation of the nucleosome-bound H1 CTD through direct protein-protein interaction rather than alterations in linker DNA trajectory. FRET-based condensation measurements, H3 tail deletion and acetylation mimic constructs, protein-protein interaction analysis on reconstituted nucleosomes Nucleic acids research Medium 33125082
2020 Single-molecule FRET revealed that H3 N-terminal tails do not diffuse freely but follow DNA motions with multiple interaction modes in the μs–ms timescale; the H3 N-tail can allosterically sense charge-modifying mutations in the histone core (H2A R81E/R88E), resulting in increased dynamic transitions and lower rate constants; H3 N-tail conformational changes coincide with DNA unwrapping steps during NaCl-induced nucleosome disassembly. High-precision single-molecule FRET on reconstituted mononucleosomes with systematic labeling position variation Nucleic acids research Medium 31956896
2020 Human FACT complex (SPT16/SSRP1) induces asymmetric conformational exposure of histone H3 N-terminal tails during nucleosome unwrapping; the pAID-side H3 tail (near the pAID-DNA hybrid) is more solvent-exposed and undergoes faster acetylation than the DNA-side H3 tail, as revealed by NMR real-time monitoring. Cryo-EM structure of FACT-nucleosome intermediate, NMR dynamics and real-time acetylation monitoring on reconstituted nucleosomes iScience High 33103079
2021 MMP-2 is the principal H3 N-terminal tail protease during skeletal myoblast differentiation, cleaving H3 between K18 and Q19; nuclear MMP-2 activity (not ECM MMP-2 activity) is required for H3NT proteolysis, myogenic gene activation, and myoblast differentiation, as demonstrated by RNAi depletion and supplementation experiments. Gelatin zymography, RNAi knockdown, ECM MMP-2 supplementation, H3 cleavage assay, myogenic differentiation assays in cell models Epigenetics & chromatin High 34001241
2021 PHD finger-containing proteins recognize the H3 N-terminal tail through a conserved mechanism requiring: (1) removal of the initiator methionine, (2) a groove for arginine-2 binding, and (3) an aromatic cage for methylated lysine-4; non-histone proteins sharing H3 N-terminal mimicry (H3TMs) can bind H3K4me3-interacting PHD domains, with VRK1 peptide binding PHF2 PHD ~3-fold stronger than H3K4me3. Protein domain microarray screening, crystal structure of PHF2 PHD bound to VRK1 K4me3 peptide, binding affinity measurements The Biochemical journal High 33969871
2021 Histone H3 N-terminal tails undergo extensive proteolytic cleavage by Trypsins and Cathepsin L in differentiated cells of the mouse intestinal villus epithelium in vivo; the PTM pattern on H3 tails differentially affects proteolytic activity of these enzymes; H3 clipping is linked to intestinal cell differentiation. Biochemical fractionation, 3D organoid cultures, in vivo mouse intestinal tissue analysis, protease identification and activity assays Nucleic acids research High 33398338
2022 In the nucleosome core particle (NCP) without linker DNA, H3 N-tail acetylation and dynamics are greatly suppressed because the H3 N-tail is strongly bound between two DNA gyres; in the chromatosome (with linker histone H1.4), the H3 N-tail adopts two conformations—one contacting two DNA gyres and one contacting linker DNA—but acetylation rates are similar to the nucleosome. H4 N-tail acetylation enhances H3 N-tail acetylation in nucleosomes by altering their mutual dynamics. NMR analysis of H3 N-tail dynamics and acetylation in NCP, nucleosome, and chromatosome reconstituted particles iScience High 35265811
2024 Cancer-associated histone H3 N-terminal arginine mutations (H3R2C and H3R26C) reduce H3K27me3 levels exclusively on the mutant histone fraction yet recurrently disrupt broad H3K27me3 domains in chromatin, disrupting PRC2 activity and leading to de-repression of differentiation pathways and impaired differentiation of mesenchymal progenitor cells. Cell-based expression of H3 mutants, ChIP-seq for H3K27me3, murine embryonic stem cell-derived teratoma differentiation assays, genomic analysis of cancer mutations Nature communications High 38886411
2024 MMP-9 mediates H3 N-terminal tail proteolysis in colon cancer cells to drive transcriptional activation of growth stimulatory genes; artificial H3NT proteolysis at target gene promoters using dCas9-MMP-9 fusion is sufficient to establish transcriptional competence, confirming that H3NT proteolysis per se (not other MMP-9 functions) is the critical epigenetic step. MMP-9 knockdown/inhibition, ChIP/ChIPac-qPCR, CRISPR/dCas9-MMP-9 targeting, genome-wide transcriptome analysis, in vivo xenograft models Molecular oncology High 38600695
2025 PHRF1 PHD finger robustly binds to the histone H3 N-terminal region; a cancer-associated mutation P221L in the PHRF1 PHD finger abolishes H3 interaction and fails to rescue defective DNA damage response (DDR) in PHRF1 knockout cells, establishing that PHRF1-H3 N-tail interaction is required for proper DDR. Biochemical binding assays, mutagenesis of PHRF1 PHD finger, PHRF1 knockout complementation, RNA-seq and proteomic analysis, DDR functional assays Nucleic acids research High 40671529
2025 HDAC1 possesses intrinsic protease activity capable of cleaving histone H3 between lysine 20 and alanine 21; this H3NT protease activity requires stable HDAC1 association with nucleosomes and is necessary for transcriptional activation of growth stimulatory genes in bladder cancer cells; artificial tethering of HDAC1 to target genes via CRISPR-dCas9 is sufficient to induce H3NT proteolysis and activate transcription. In vitro and cellular H3 cleavage assays, HDAC1 knockdown, CRISPR-dCas9 tethering, cancer cell proliferation assays Cell death and differentiation High 41286098
2023 MMP-2 H3NT protease is selectively localized to transcription start sites (TSSs) of highly expressed protein-coding genes at the +1 nucleosome genome-wide; MMP-2-dependent H3NT proteolysis at TSSs results in >2-fold reduction of H3K4me3, H3K9ac, and H3K18ac; MMP-2-mediated H3NT proteolysis activates CTSB, which functions as a secondary nuclear H3NT protease generating additional cleaved H3 products. ChIP-seq for MMP-2 genome-wide localization, H3 cleavage assays, histone PTM analysis by ChIP-qPCR Epigenetics & chromatin High 37161413
2025 Histone H3 threonine 3 (H3T3) phosphorylation is required for meiotic division in yeast; H3T3A substitution reduces sporulation efficiency and spore viability; deletion of MAD2 (spindle checkpoint gene) in the H3T3A mutant severely reduces spore viability, indicating the spindle checkpoint monitors H3T3-dependent functions during meiosis. Yeast genetic mutagenesis (T3A, K4A, S10A substitutions), sporulation efficiency and spore viability quantification, MAD2 deletion epistasis Biomolecules Medium 40867646

Source papers

Stage 0 corpus · 28 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1992 Histone H3 N-terminal mutations allow hyperactivation of the yeast GAL1 gene in vivo. The EMBO journal 164 1505519
2004 Redundant roles for histone H3 N-terminal lysine residues in subtelomeric gene repression in Saccharomyces cerevisiae. Genetics 54 15280228
2017 JMJD5 cleaves monomethylated histone H3 N-tail under DNA damaging stress. EMBO reports 50 28982940
2009 Histone H3 N-terminus regulates higher order structure of yeast heterochromatin. Proceedings of the National Academy of Sciences of the United States of America 47 19666585
2020 Dynamics of the nucleosomal histone H3 N-terminal tail revealed by high precision single-molecule FRET. Nucleic acids research 37 31956896
2008 Effects of posttranslational modifications on the structure and dynamics of histone H3 N-terminal Peptide. Biophysical journal 34 18192367
2021 Intestinal differentiation involves cleavage of histone H3 N-terminal tails by multiple proteases. Nucleic acids research 27 33398338
2014 PRB1 is required for clipping of the histone H3 N terminal tail in Saccharomyces cerevisiae. PloS one 26 24587380
2007 T-box factors: targeting to chromatin and interaction with the histone H3 N-terminal tail. Pigment cell research 23 17630961
2019 DNMT and HDAC inhibitors modulate MMP-9-dependent H3 N-terminal tail proteolysis and osteoclastogenesis. Epigenetics & chromatin 20 30992059
2020 Acetylation-modulated communication between the H3 N-terminal tail domain and the intrinsically disordered H1 C-terminal domain. Nucleic acids research 19 33125082
2020 Partial Replacement of Nucleosomal DNA with Human FACT Induces Dynamic Exposure and Acetylation of Histone H3 N-Terminal Tails. iScience 15 33103079
2015 The histone H3 N-terminal tail: a computational analysis of the free energy landscape and kinetics. Physical chemistry chemical physics : PCCP 15 25942635
2021 MMP-2 is a novel histone H3 N-terminal protease necessary for myogenic gene activation. Epigenetics & chromatin 13 34001241
2011 Methylation-mediated control of aurora kinase B and Haspin with epigenetically modified histone H3 N-terminal peptides. Bioorganic & medicinal chemistry 13 21397507
2016 Histone H3 N-terminal acetylation sites especially K14 are important for rDNA silencing and aging. Scientific reports 11 26906758
2011 An RNA aptamer that selectively recognizes symmetric dimethylation of arginine 8 in the histone H3 N-terminal peptide. Nucleic acid therapeutics 11 21749292
2022 Characteristic H3 N-tail dynamics in the nucleosome core particle, nucleosome, and chromatosome. iScience 9 35265811
2014 Reptin and Pontin oligomerization and activity are modulated through histone H3 N-terminal tail interaction. The Journal of biological chemistry 9 25336637
2024 MMP-9-dependent proteolysis of the histone H3 N-terminal tail: a critical epigenetic step in driving oncogenic transcription and colon tumorigenesis. Molecular oncology 8 38600695
2024 Cancer-associated Histone H3 N-terminal arginine mutations disrupt PRC2 activity and impair differentiation. Nature communications 7 38886411
2021 Histone H3 N-terminal mimicry drives a novel network of methyl-effector interactions. The Biochemical journal 7 33969871
2009 Histone H3 N-terminal peptide binds directly to its own mRNA: a possible mode of feedback inhibition to control translation. Chembiochem : a European journal of chemical biology 7 19405068
2023 The MMP-2 histone H3 N-terminal tail protease is selectively targeted to the transcription start sites of active genes. Epigenetics & chromatin 5 37161413
2025 Histone H3 N-terminal recognition by the PHD finger of PHRF1 is required for proper DNA damage response. Nucleic acids research 2 40671529
2025 Histone H3 N-Terminal Tail Residues Important for Meiosis in Saccharomyces cerevisiae. Biomolecules 0 40867646
2025 HDAC1 has intrinsic protease activity and regulates transcription through clipping histone H3 N-terminal tail. Cell death and differentiation 0 41286098
2024 Histone H3 N-terminal recognition by the PHD finger of PHRF1 is required for proper DNA damage response. bioRxiv : the preprint server for biology 0 39605374

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