| 1990 |
Two specific seven-amino-acid segments from yeast ribosomal protein L29 function as nuclear localizing sequences (NLS); basic residues, especially a particular Arg residue, are critical for nuclear localization. Arg→Lys substitution in the proximal NLS greatly reduced ribosome assembly and cell growth, and substitution in both NLS caused a still greater defect, placing these sequences as necessary for both nuclear import and ribosome assembly. |
Reporter protein fusion, mutagenesis (Arg→Lys substitutions), yeast growth assays, ribosome assembly analysis |
The EMBO journal |
High |
2104804
|
| 1980 |
A mutation in the structural gene for yeast ribosomal protein L29 confers cycloheximide resistance, demonstrating that L29 is the target of cycloheximide action in the large (60S) ribosomal subunit. |
Two-dimensional gel electrophoresis of ribosomal proteins, genetic co-segregation analysis in yeast |
Current genetics |
Medium |
24189656
|
| 1982 |
The yeast cycloheximide resistance gene CYH2 encodes ribosomal protein L29, a component of the large (60S) subunit; the gene is present as a single copy and contains an intervening sequence. |
Molecular cloning, cross-hybridization, blot hybridization |
Nucleic acids research |
Medium |
6285288
|
| 1981 |
E. coli ribosomal protein L29 is cross-linked to positions 99–107 of 23S rRNA in the 50S subunit, placing L29 in direct contact with this specific rRNA region. |
RNA-protein cross-linking with 2-iminothiolane followed by UV irradiation; RNA fragment identification |
Nucleic acids research |
Medium |
6170935
|
| 1985 |
A mutant E. coli lacking ribosomal proteins S17 and L29 was used to localize L29 to the back of the 50S subunit, on the opposite side from the subunit interface, by immunoelectron microscopy. |
Isolation of deletion mutant, immunological localization on ribosomal surface by electron microscopy |
European journal of biochemistry |
Medium |
3926498
|
| 1984 |
Ribosomal proteins L6 and L29 occupy closely adjacent sites in mammalian 60S subunits and can be cross-linked via intermolecular disulfide bonds; the interacting cysteine of L29 is located approximately 40 residues from its C-terminus. |
Disulfide cross-linking, S-cleavage after cyanylation, polyacrylamide gel electrophoresis, autoradiography |
European journal of biochemistry |
Medium |
6468376
|
| 1993 |
In Bacillus stearothermophilus ribosomes, cross-linking with diepoxybutane identified L23 and L29 as neighboring proteins; the cross-link involved Met-1 of L23 and Lys-4 of L29. |
Chemical cross-linking with diepoxybutane, protein isolation, sequence analysis and mass spectrometry |
The Journal of biological chemistry |
Medium |
8444837
|
| 1998 |
Murine HIP/RPL29 (identical to ribosomal protein L29) is enriched in the 100,000×g particulate (membrane) fraction of mammary epithelial cells and behaves as a peripheral membrane protein (eluted with 0.8 M NaCl); recombinant murine HIP/RPL29 binds heparin directly and selectively compared to other glycosaminoglycans. |
Cell fractionation, salt extraction, gel overlay binding assay with 125I-heparin, heparin-agarose affinity chromatography with glycosaminoglycan competition |
The Journal of biological chemistry |
High |
9737974
|
| 2000 |
Multiple distinct domains of human and murine HIP/RPL29 contribute to heparin/heparan sulfate (Hp/HS) binding; heparin binding induces a conformational change in human HIP/RPL29 detected by circular dichroism spectroscopy. |
Deletion mutants, proteolytic fragments, protease-protection assays, circular dichroism spectroscopy |
Biochemistry |
High |
11123893
|
| 2002 |
Deletion of yeast RPL29 causes accumulation of half-mer polysomes and impaired 60S-to-40S subunit joining; synthetic lethality with RPL10 (essential for subunit joining) and RSA1 (required for Rpl10 loading onto 60S), and RPL10 over-expression suppresses the half-mer phenotype, placing RPL29 as a facilitator of proper 60S subunit assembly and ribosomal subunit joining. |
Gene deletion, polysome profiling, in vitro translation, synthetic lethality epistasis analysis, gene over-expression suppression assay |
Biochimica et biophysica acta |
High |
11997090
|
| 1989 |
Mouse ribosomal protein L27' (ortholog of yeast L29) can functionally substitute for yeast L29 in yeast ribosomes (supporting normal growth in L29-null cells), but is outcompeted when yeast L29 is also present, demonstrating evolutionary conservation of ribosomal function. |
cDNA expression in yeast, cycloheximide sensitivity assay, growth complementation assay in L29-null yeast |
Proceedings of the National Academy of Sciences of the United States of America |
High |
2643099
|
| 2007 |
HIP/RPL29-null mice are viable but show global growth reduction (~50% smaller), delayed embryonic growth from mid-gestation, decreased proliferation and protein synthesis in embryonic fibroblasts, and reduced steady-state levels of core ribosomal proteins, establishing RPL29 as a regulator of global protein synthesis rate. |
Gene targeting/knockout mice, phenotypic analysis, cell proliferation assays, protein synthesis measurement, Western blotting for core RPs |
Developmental dynamics |
High |
17195189
|
| 2006 |
Knockdown of HIP/RPL29 by siRNA in LS174T colon cancer cells induces cellular differentiation (upregulation of galectin-4 and mucin-2 markers) accompanied by upregulation of p21 and p53, placing RPL29 in a pathway that suppresses differentiation through p21/p53. |
siRNA knockdown, marker expression analysis (galectin-4, mucin-2), Western blot for p21/p53 |
Journal of cellular physiology |
Medium |
16475173
|
| 2003 |
Ribozyme-mediated partial knockdown of HIP/RPL29 in C3H/10T(1/2) multipotent cells accelerates differentiation into cartilage-like cells, demonstrating that HIP/RPL29 expression maintains chondrocyte proliferation and opposes differentiation. |
Ribozyme-mediated knockdown, chondrogenic differentiation assay, histochemical and molecular marker analysis |
Differentiation; research in biological diversity |
Medium |
12919102
|
| 2008 |
HIP/RPL29 inhibits VEGF- and FGF2-stimulated angiogenesis by displacing HS-bound growth factors from perlecan domain I and antagonizing heparanase (HPSE) activity (inhibiting soluble HS release); partial inhibition of VEGFR2 phosphorylation at Y951 (migration-associated site) was also observed. |
Endothelial tube formation assay, aortic explant assay, HBGF displacement from HS-bearing perlecan, HPSE activity assay, Western blot for receptor phosphorylation |
Journal of cellular biochemistry |
Medium |
18980226
|
| 2002 |
Recombinant HIP/RPL29 inhibits bFGF-induced proliferation of gingival fibroblasts and specifically blocks bFGF stimulation of p44 (Erk-1) MAPK phosphorylation in a dose-dependent manner, without affecting IGF-1 responses, indicating that HIP/RPL29 modulates bFGF bioavailability via HS interactions. |
Cell proliferation assay, Western blot for MAPK phosphorylation, dose-response analysis with recombinant HIP/RPL29 |
Journal of dental research |
Medium |
12097308
|
| 2012 |
RPL29 regulates tumour angiogenesis in vivo: VEGF-stimulated microvessel sprouting is significantly reduced in Rpl29-heterozygous and Rpl29-null aortic ring assays ex vivo, and tumour blood vessel density is reduced in Rpl29-mutant mice bearing Lewis lung carcinomas; siRNA depletion of Rpl29 also inhibits VEGF-induced sprouting. |
Rpl29 heterozygous/null mouse models, ex vivo aortic ring sprouting assay, in vivo tumour implantation, siRNA knockdown, immunohistochemistry for vessel density |
Disease models & mechanisms |
High |
23118343
|
| 2018 |
Ribosomal protein RPL29/eL29 is a major substrate of the lysine methyltransferase Set7/9; RPL29 lysine 5 (Rpl29K5) is methylated exclusively by Set7/9 and can be demethylated by Lsd1/Kdm1a. Methylation at K5 does not affect global protein synthesis but alters RPL29 subcellular localization. |
Mass spectrometry substrate identification, methyltransferase assay with Set7/9 and mutants, methylation-specific antibody validation, Set7/9 inhibitor ((R)-PFI-2) treatment, subcellular localization analysis |
The Journal of biological chemistry |
High |
29959229
|
| 2018 |
Isotopically labeled RPL29 can be reconstituted into the 50S large ribosomal subunit; RPL29 is located at the exit of the polypeptide tunnel of the 50S subunit and can undergo allosteric conformational changes induced by the nascent polypeptide chain, potentially triggering interactions with chaperones (trigger factor or SRP). |
Isotopic labeling, in vitro reconstitution into 50S subunit, solid-state and solution NMR |
Methods in molecular biology |
Medium |
29605910
|
| 2020 |
Human ribosomal protein eL29 (RPL29) binds its own cognate mRNA in cells at the 3' part of the coding sequence (CDS), mimicking its rRNA binding site; overproduced eL29 inhibits translation of the eL29 mRNA CDS transcript in a cell-free system and co-immunoprecipitates with eL29 mRNA from ribosome-depleted lysate, establishing a feedback autoregulation of eL29 synthesis. |
4-thiouridine-enhanced CLIP (PAR-CLIP) in HEK293T cells, next-generation sequencing, co-immunoprecipitation of mRNA, cell-free translation inhibition assay |
Biochimie |
High |
32798643
|
| 2002 |
HIP/RPL29 intracellular distribution shifts between nuclear and cytoplasmic compartments depending on mammary epithelial cell growth/differentiation state (nuclear in proliferating/differentiating cells, cytoplasmic in mature secretory cells), as confirmed by GFP-fusion protein live imaging. |
Immunohistochemistry, cell fractionation, GFP-fusion protein transfection and live imaging in NMuMG cells |
Developmental dynamics |
Medium |
11803571
|
| 1998 |
E. coli ribosomal protein L29 and acyl carrier protein (ACP) together stimulate binding of TnsD to the Tn7 attachment site (attTn7) and stimulate Tn7 transposition in vitro; mutations in L29 drastically decrease Tn7 transposition in vivo specifically for TnsABC+D reactions. |
In vitro transposition assay, TnsD binding assay, L29 mutant analysis in vivo |
The EMBO journal |
Medium |
9755182
|
| 2025 |
RPL29 mRNA is a direct target of IGF2BP1/3 (m6A readers) in a METTL14-dependent manner; luciferase reporter assays showed increased mRNA stability of the RPL29 3'-UTR upon co-expression of IGF2BP1/3 and METTL3/14, indicating that m6A modification promotes IGF2BP1/3-mediated stabilization of RPL29 mRNA. |
eCLIP data intersection analysis, 3'-UTR luciferase reporter assay, IGF2BP1/3 and METTL3/14 overexpression |
bioRxiv (preprint)preprint |
Low |
bio_10.1101_2025.05.04.652102
|