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RPL10
Introduction
Ribosomal protein L10, also known as RPL10, is a human gene.[1]
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L10E family of ribosomal proteins. It is located in the cytoplasm. In vitro studies have shown that the chicken protein can bind to c-Jun and can repress c-Jun-mediated transcriptional activation, but these activities have not been demonstrated in vivo. This gene was initially identified as a candidate for a Wilms tumor suppressor gene, but later studies determined that this gene is not involved in the suppression of Wilms tumor. This gene has been referred to as ‘laminin receptor homolog’ because a chimeric transcript consisting of sequence from this gene and sequence from the laminin receptor gene was isolated; however, it is not believed that this gene encodes a laminin receptor. Transcript variants utilizing alternative polyA signals exist. The variant with the longest 3′ UTR overlaps the deoxyribonuclease I-like 1 gene on the opposite strand. This gene is co-transcribed with the small nucleolar RNA gene U70, which is located in its fifth intron. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[1]
Further reading
Further reading
- Wool IG, Chan YL, GlΓΌck A (1996). “Structure and evolution of mammalian ribosomal proteins”. Biochem. Cell Biol. 73 (11β12): 933β47. PMIDΒ 8722009.
- van den Ouweland AM, Kioschis P, Verdijk M; et al. (1993). “Identification and characterization of a new gene in the human Xq28 region”. Hum. Mol. Genet. 1 (4): 269β73. PMIDΒ 1303197.
- van den Ouweland AM, Verdijk M, Mannens MM, van Oost BA (1992). “The QM gene is X-linked and therefore not involved in suppression of tumorigenesis in Wilms’ tumor”. Hum. Genet. 90 (1β2): 144β6. PMIDΒ 1330878.
- Kaneko K, Kobayashi H, Onodera O; et al. (1993). “Genomic organization of a cDNA (QM) demonstrating an altered mRNA level in nontumorigenic Wilms’ microcell hybrid cells and its localization to Xq28”. Hum. Mol. Genet. 1 (7): 529β33. PMIDΒ 1339145.
- Bignon C, Roux-Dosseto M, Zeigler ME; et al. (1992). “cDNA cloning and genomic analysis of a new multigene family sharing common phylogenetic and expression profiles with the laminin receptor gene”. Biochem. Biophys. Res. Commun. 184 (3): 1165β72. PMIDΒ 1534224.
- Dowdy SF, Lai KM, Weissman BE; et al. (1991). “The isolation and characterization of a novel cDNA demonstrating an altered mRNA level in nontumorigenic Wilms’ microcell hybrid cells”. Nucleic Acids Res. 19 (20): 5763β9. PMIDΒ 1658743.
- Kato S, Sekine S, Oh SW; et al. (1995). “Construction of a human full-length cDNA bank”. Gene. 150 (2): 243β50. PMIDΒ 7821789.
- Matoba R, Okubo K, Hori N; et al. (1994). “The addition of 5′-coding information to a 3′-directed cDNA library improves analysis of gene expression”. Gene. 146 (2): 199β207. PMIDΒ 8076819.
- Maruyama K, Sugano S (1994). “Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene. 138 (1β2): 171β4. PMIDΒ 8125298.
- Farmer AA, Johnsen JI, Loftus TM; et al. (1996). “Isolation and characterization of the QM promoter”. Nucleic Acids Res. 24 (11): 2158β65. PMIDΒ 8668549.
- Chen EY, Zollo M, Mazzarella R; et al. (1997). “Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci”. Hum. Mol. Genet. 5 (5): 659β68. PMIDΒ 8733135.
- Chan YL, Diaz JJ, Denoroy L; et al. (1996). “The primary structure of rat ribosomal protein L10: relationship to a Jun-binding protein and to a putative Wilms’ tumor suppressor”. Biochem. Biophys. Res. Commun. 225 (3): 952β6. doi:10.1006/bbrc.1996.1277. PMIDΒ 8780716.
- Inada H, Mukai J, Matsushima S, Tanaka T (1997). “QM is a novel zinc-binding transcription regulatory protein: its binding to c-Jun is regulated by zinc ions and phosphorylation by protein kinase C.”. Biochem. Biophys. Res. Commun. 230 (2): 331β4. doi:10.1006/bbrc.1996.5955. PMIDΒ 9016777.
- Loftus TM, Nguyen YH, Stanbridge EJ (1997). “The QM protein associates with ribosomes in the rough endoplasmic reticulum”. Biochemistry. 36 (27): 8224β30. doi:10.1021/bi970288d. PMIDΒ 9204867.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). “Construction and characterization of a full length-enriched and a 5′-end-enriched cDNA library”. Gene. 200 (1β2): 149β56. PMIDΒ 9373149.
- Nguyen YH, Mills AA, Stanbridge EJ (1998). “Assembly of the QM protein onto the 60S ribosomal subunit occurs in the cytoplasm”. J. Cell. Biochem. 68 (2): 281β5. PMIDΒ 9443083.
- Kenmochi N, Kawaguchi T, Rozen S; et al. (1998). “A map of 75 human ribosomal protein genes”. Genome Res. 8 (5): 509β23. PMIDΒ 9582194.
- Hartley JL, Temple GF, Brasch MA (2001). “DNA cloning using in vitro site-specific recombination”. Genome Res. 10 (11): 1788β95. PMIDΒ 11076863.
- Simpson JC, Wellenreuther R, Poustka A; et al. (2001). “Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing”. EMBO Rep. 1 (3): 287β92. doi:10.1093/embo-reports/kvd058. PMIDΒ 11256614.
