40S ribosomal protein S27a is a protein that in humans is encoded by the RPS27A gene.[5][6]
Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein S27a at the C terminus. When expressed in yeast, the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the ribosome and belongs to the S27AE family of ribosomal proteins. It contains C4-type zinc finger domains and is located in the cytoplasm. Pseudogenes derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesized as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesized as a fusion protein with the ubiquitin-like protein fubi.[6]
References[edit]
- ^ a b c GRCh38: Ensembl release 89: ENSG00000143947 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020460 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (Aug 1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.
- ^ a b "Entrez Gene: RPS27A ribosomal protein S27a".
Further reading[edit]
- Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID 8722009.
- Adams SM, Sharp MG, Walker RA, et al. (1992). "Differential expression of translation-associated genes in benign and malignant human breast tumours". Br. J. Cancer. 65 (1): 65–71. doi:10.1038/bjc.1992.12. PMC 1977345. PMID 1370760.
- Pancré V, Pierce RJ, Fournier F, et al. (1991). "Effect of ubiquitin on platelet functions: possible identity with platelet activity suppressive lymphokine (PASL)". Eur. J. Immunol. 21 (11): 2735–41. doi:10.1002/eji.1830211113. PMID 1657614. S2CID 23901646.
- Kanayama H, Tanaka K, Aki M, et al. (1992). "Changes in expressions of proteasome and ubiquitin genes in human renal cancer cells". Cancer Res. 51 (24): 6677–85. PMID 1660345.
- Monia BP, Ecker DJ, Jonnalagadda S, et al. (1989). "Gene synthesis, expression, and processing of human ubiquitin carboxyl extension proteins". J. Biol. Chem. 264 (7): 4093–103. doi:10.1016/S0021-9258(19)84967-0. PMID 2537304.
- Redman KL, Rechsteiner M (1989). "Identification of the long ubiquitin extension as ribosomal protein S27a". Nature. 338 (6214): 438–40. Bibcode:1989Natur.338..438R. doi:10.1038/338438a0. PMID 2538756. S2CID 4360107.
- Lund PK, Moats-Staats BM, Simmons JG, et al. (1985). "Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor". J. Biol. Chem. 260 (12): 7609–13. doi:10.1016/S0021-9258(17)39652-7. PMID 2581967.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Vladimirov SN, Ivanov AV, Karpova GG, et al. (1996). "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry". Eur. J. Biochem. 239 (1): 144–9. doi:10.1111/j.1432-1033.1996.0144u.x. PMID 8706699.
- 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 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Kirschner LS, Stratakis CA (2000). "Structure of the human ubiquitin fusion gene Uba80 (RPS27a) and one of its pseudogenes". Biochem. Biophys. Res. Commun. 270 (3): 1106–10. doi:10.1006/bbrc.2000.2568. PMID 10772958.
- Petersen BO, Wagener C, Marinoni F, et al. (2000). "Cell cycle– and cell growth–regulated proteolysis of mammalian CDC6 is dependent on APC–CDH1". Genes Dev. 14 (18): 2330–43. doi:10.1101/gad.832500. PMC 316932. PMID 10995389.
- Bolton D, Evans PA, Stott K, Broadhurst RW (2002). "Structure and properties of a dimeric N-terminal fragment of human ubiquitin". J. Mol. Biol. 314 (4): 773–87. doi:10.1006/jmbi.2001.5181. PMID 11733996.
- Yoshihama M, Uechi T, Asakawa S, et al. (2002). "The Human Ribosomal Protein Genes: Sequencing and Comparative Analysis of 73 Genes". Genome Res. 12 (3): 379–90. doi:10.1101/gr.214202. PMC 155282. PMID 11875025.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Cohen BD, Bariteau JT, Magenis LM, Dias JA (2003). "Regulation of follitropin receptor cell surface residency by the ubiquitin-proteasome pathway". Endocrinology. 144 (10): 4393–402. doi:10.1210/en.2002-0063. PMID 12960054.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Li H, Seth A (2004). "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein". Oncogene. 23 (10): 1801–8. doi:10.1038/sj.onc.1207319. PMID 14755250. S2CID 37253372.