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Gene Review

RPS27A  -  ribosomal protein S27a

Gallus gallus

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Disease relevance of RPS27A


High impact information on RPS27A


Biological context of RPS27A


Anatomical context of RPS27A

  • Multiple ubiquitin C-terminal hydrolases from chick skeletal muscle [12].
  • Previously, we isolated an ATP-dependent proteolytic pathway in muscle, liver, and reticulocytes that requires ubiquitin and the enzymes which conjugate ubiquitin to proteins [13].
  • Ubiquitin, a small 76-amino acid protein which is highly conserved in eukaryotic cells, occurs in several forms other than the free polypeptide [4].
  • Similarly, in HeLa cell extracts aged CaM was degraded at a higher rate, even though it was not conjugated to ubiquitin more rapidly than the native species [14].
  • Inasmuch as cleavage of the ubiquitin---histone 2A bond of protein A24 and loss of ubiquitin accompanied transcriptional shutdown during erythropoiesis, the presence of protein A24 and ubiquitin in premature polychromatic erythrocytes may reflect the presence of potentially active and transcribing chromatin structures [11].

Associations of RPS27A with chemical compounds

  • The extreme conservatism of ubiquitin evolution also allows the inference that certain synonymous serine codons differing at the first two positions were probably mutated at single steps [15].
  • Like other UCHs it was sensitive to inhibition by thiol-blocking agents such as N-ethylmaleimide, and by ubiquitin aldehyde [16].
  • Cell suspensions were fractionated on albumin gradients to remove nonlymphoid cells and incubated in vitro with bursopoietin, a specific inducer of B cells, or crude chicken thymus extract, a specific inducer of T cells, or ubiquitin, a nonspecific inducer [17].
  • Thus, an important component of muscle proteolysis inhibition by leucine, through the PI3K and PKC, is its ability to suppress transcription of the ubiquitin and proteasome C2 subunit, and degradation of myofibrillar protein [18].
  • In chick myotubes, leucine suppressed myofibrillar proteolysis (as measured by N(tau)-methylhistidine release), while also decreasing ubiquitin and proteasome C2 subunit mRNA [18].

Regulatory relationships of RPS27A


Other interactions of RPS27A

  • UBP41 also released free ubiquitin from poly-His-tagged di-ubiquitin [20].
  • Moreover, overexpression of b-catenin caused degradation of Sox9 via the ubiquitin/26S proteasome pathway [21].
  • Both the rate and the extent of ubiquitin-lysozyme conjugation, however, are significantly higher with this modified substrate [22].
  • In addition, UCH-1 and UCH-7 could remove ubiquitin that had been ligated covalently by an isopeptide linkage to a ubiquitin (RGA)-alpha NH-peptide, the peptide portion of which consists of the 20 amino acids of the calmodulin binding domain of myosin light chain kinase [12].
  • Effect of high mobility group nonhistone proteins HMG-20 (ubiquitin) and HMG-17 on histone deacetylase activity assayed in vitro [19].

Analytical, diagnostic and therapeutic context of RPS27A


  1. The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Ciechanover, A., Brundin, P. Neuron (2003) [Pubmed]
  2. Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cells. Kikonyogo, A., Bouamr, F., Vana, M.L., Xiang, Y., Aiyar, A., Carter, C., Leis, J. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  3. Small ubiquitin-related modifiers: A novel and independent class of autoantigens in primary biliary cirrhosis. Janka, C., Selmi, C., Gershwin, M.E., Will, H., Sternsdorf, T. Hepatology (2005) [Pubmed]
  4. Ubiquitin in stressed chicken embryo fibroblasts. Bond, U., Agell, N., Haas, A.L., Redman, K., Schlesinger, M.J. J. Biol. Chem. (1988) [Pubmed]
  5. Cloning and developmental expression of a chick G-protein-coupled receptor SCGPR1. Odani, N., Pfaff, S.L., Nakamura, H., Funahashi, J. Gene Expr. Patterns (2007) [Pubmed]
  6. Ubiquitin-mediated degradation of active Src tyrosine kinase. Harris, K.F., Shoji, I., Cooper, E.M., Kumar, S., Oda, H., Howley, P.M. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  7. c-myc and c-myb protein degradation: effect of metabolic inhibitors and heat shock. Lüscher, B., Eisenman, R.N. Mol. Cell. Biol. (1988) [Pubmed]
  8. The chicken ubiquitin gene contains a heat shock promoter and expresses an unstable mRNA in heat-shocked cells. Bond, U., Schlesinger, M.J. Mol. Cell. Biol. (1986) [Pubmed]
  9. Ubiquitin is a heat shock protein in chicken embryo fibroblasts. Bond, U., Schlesinger, M.J. Mol. Cell. Biol. (1985) [Pubmed]
  10. Characterization and expression of two chicken cDNAs encoding ubiquitin fused to ribosomal proteins of 52 and 80 amino acids. Mezquita, J., Pau, M., Mezquita, C. Gene (1997) [Pubmed]
  11. Chromatin conjugate protein A24 is cleaved and ubiquitin is lost during chicken erythropoiesis. Goldknopf, I.L., Wilson, G., Ballal, N.R., Busch, H. J. Biol. Chem. (1980) [Pubmed]
  12. Multiple ubiquitin C-terminal hydrolases from chick skeletal muscle. Woo, S.K., Lee, J.I., Park, I.K., Yoo, Y.J., Cho, C.M., Kang, M.S., Ha, D.B., Tanaka, K., Chung, C.H. J. Biol. Chem. (1995) [Pubmed]
  13. A novel ATP-requiring protease from skeletal muscle that hydrolyzes non-ubiquitinated proteins. Fagan, J.M., Waxman, L. J. Biol. Chem. (1989) [Pubmed]
  14. Ca2+-free calmodulin and calmodulin damaged by in vitro aging are selectively degraded by 26 S proteasomes without ubiquitination. Tarcsa, E., Szymanska, G., Lecker, S., O'Connor, C.M., Goldberg, A.L. J. Biol. Chem. (2000) [Pubmed]
  15. Ubiquitin genes as a paradigm of concerted evolution of tandem repeats. Sharp, P.M., Li, W.H. J. Mol. Evol. (1987) [Pubmed]
  16. New de-ubiquitinating enzyme, ubiquitin C-terminal hydrolase 8, in chick skeletal muscle. Baek, S.H., Woo, S.K., Lee, J.I., Yoo, Y.J., Cho, C.M., Kang, M.S., Tanaka, K., Chung, C.H. Biochem. J. (1997) [Pubmed]
  17. Committed precursors of B and T lymphocytes in chick embryo bursa of Fabricius, thymus, and bone marrow. Brand, A., Galton, J., Gilmour, D.G. Eur. J. Immunol. (1983) [Pubmed]
  18. Leucine suppresses myofibrillar proteolysis by down-regulating ubiquitin-proteasome pathway in chick skeletal muscles. Nakashima, K., Ishida, A., Yamazaki, M., Abe, H. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  19. Effect of high mobility group nonhistone proteins HMG-20 (ubiquitin) and HMG-17 on histone deacetylase activity assayed in vitro. Mezquita, J., Chiva, M., Vidal, S., Mezquita, C. Nucleic Acids Res. (1982) [Pubmed]
  20. Molecular cloning of a novel ubiquitin-specific protease, UBP41, with isopeptidase activity in chick skeletal muscle. Baek, S.H., Choi, K.S., Yoo, Y.J., Cho, J.M., Baker, R.T., Tanaka, K., Chung, C.H. J. Biol. Chem. (1997) [Pubmed]
  21. BMP-2-Enhanced Chondrogenesis Involves p38 MAPK-mediated Down-Regulation of Wnt-7a Pathway. Jin, E.J., Lee, S.Y., Choi, Y.A., Jung, J.C., Bang, O.S., Kang, S.S. Mol. Cells (2006) [Pubmed]
  22. Specific disulfide cleavage is required for ubiquitin conjugation and degradation of lysozyme. Dunten, R.L., Cohen, R.E., Gregori, L., Chau, V. J. Biol. Chem. (1991) [Pubmed]
  23. A branched, synthetic octapeptide of ubiquitinated histone H2A as target of autoantibodies. Plaué, S., Muller, S., van Regenmortel, M.H. J. Exp. Med. (1989) [Pubmed]
  24. Assembly of semihistone A24. Trempe, J., Leffak, M. Nucleic Acids Res. (1982) [Pubmed]
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