Divergence and conservation of SUP2 (SUP35) gene of yeast Pichia pinus and Saccharomyces cerevisiae - PubMed

Affiliations

• PMID: 2080663
• DOI: 10.1002/yea.320060603

Divergence and conservation of SUP2 (SUP35) gene of yeast Pichia pinus and Saccharomyces cerevisiae

V V Kushnirov et al. Yeast. 1990 Nov-Dec.

Abstract

SUP2 (SUP35) is an omnipotent suppressor gene, coding for an EF-1 alpha-like protein factor, intimately involved in the control of translational accuracy in yeast Saccharomyces cerevisiae. In the present study a SUP2 gene analogue from yeast Pichia pinus was isolated by complementation of the temperature-sensitive sup2 mutation of S. cerevisiae. The nucleotide sequence of the SUP2 gene of P. pinus codes for a protein of 82.4 kDa, exceeding the Sup2 protein of S. cerevisiae by 6 kDa. Like the SUP2 gene product of S. cerevisiae, the Sup2 protein of P. pinus represents a fusion of a unique N-terminal part and a region homologous to EF-1 alpha. The comparison of amino acid sequences of the Sup2 proteins reveals high conservation (76%) of the C-terminal region and low conservation (36%) of the N-terminal part where, in addition, the homologous correspondence is ambiguous. Proteins related to the Sup2 of S. cerevisiae were found in P. pinus and some other yeast species by the immunoblotting technique. The relation between the evolutionary conservation of different regions of the Sup2 protein and their functional significance is discussed.

Similar articles

• [Comparative analysis of the structure of SUP2 genes in Pichia pinus and Saccharomyces cerevisiae].

  Kushnirov VV, Ter-Avanesian MD, Smirnov VN, Chernov IuO, Derkach IL, Novikova ON, Inge-Vechtomov SG, Neĭstat MA, Tolstorukov II. Kushnirov VV, et al. Mol Biol (Mosk). 1990 Jul-Aug;24(4):1024-36. Mol Biol (Mosk). 1990. PMID: 2250670 Russian.

• [Prionization of the Pichia methanolica SUP35 gene product in the yeast Saccharomyces cerevisiae].

  Zadorskiĭ SP, Sopova IuV, Inge-Vechtomov SG. Zadorskiĭ SP, et al. Genetika. 2000 Oct;36(10):1322-9. Genetika. 2000. PMID: 11094743 Russian.

• [Deletion analysis of the SUP2 gene in Saccharomyces cerevisiae].

  Kushnirov VV, Ter-Avanesian MD, Dagkesamanskaia AR, Chernov IuO, Inge-Vechtomov SG, Smirnov VN. Kushnirov VV, et al. Mol Biol (Mosk). 1990 Jul-Aug;24(4):1037-41. Mol Biol (Mosk). 1990. PMID: 2250671 Russian.

• [Molecular biology of yeast prions].

  Nakayashiki T, Nakamura Y. Nakayashiki T, et al. Uirusu. 2001 Dec;51(2):171-6. Uirusu. 2001. PMID: 11977758 Review. Japanese. No abstract available.

• Conservative system for dosage-dependent modulation of translational fidelity in eukaryotes.

  Chernoff YO, Ptyushkina MV, Samsonova MG, Sizonencko GI, Pavlov YI, Ter-Avanesyan MD, Inge-Vechtomov SG. Chernoff YO, et al. Biochimie. 1992 May;74(5):455-61. doi: 10.1016/0300-9084(92)90086-t. Biochimie. 1992. PMID: 1637871 Review.

Cited by

• A deletion polymorphism in the human alpha-2-macroglobulin (A2M) gene.

  Matthijs G, Marynen P. Matthijs G, et al. Nucleic Acids Res. 1991 Sep 25;19(18):5102. doi: 10.1093/nar/19.18.5102. Nucleic Acids Res. 1991. PMID: 1717945 Free PMC article.

• Structure comparison and evolutionary relations between elongation factors EF-Tu (EF-1 alpha) and SUP 2 proteins.

  Samsonova MG, Inge-Vechtomov SG, Taylor P. Samsonova MG, et al. Genetica. 1991;85(1):35-44. doi: 10.1007/BF00056104. Genetica. 1991. PMID: 1778473

• Mammalian amyloidogenic proteins promote prion nucleation in yeast.

  Chandramowlishwaran P, Sun M, Casey KL, Romanyuk AV, Grizel AV, Sopova JV, Rubel AA, Nussbaum-Krammer C, Vorberg IM, Chernoff YO. Chandramowlishwaran P, et al. J Biol Chem. 2018 Mar 2;293(9):3436-3450. doi: 10.1074/jbc.M117.809004. Epub 2018 Jan 12. J Biol Chem. 2018. PMID: 29330303 Free PMC article.

• Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants.

  Dergalev AA, Alexandrov AI, Ivannikov RI, Ter-Avanesyan MD, Kushnirov VV. Dergalev AA, et al. Int J Mol Sci. 2019 May 29;20(11):2633. doi: 10.3390/ijms20112633. Int J Mol Sci. 2019. PMID: 31146333 Free PMC article.

• Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3.

  Zhouravleva G, Frolova L, Le Goff X, Le Guellec R, Inge-Vechtomov S, Kisselev L, Philippe M. Zhouravleva G, et al. EMBO J. 1995 Aug 15;14(16):4065-72. doi: 10.1002/j.1460-2075.1995.tb00078.x. EMBO J. 1995. PMID: 7664746 Free PMC article.

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Wiley

• Other Literature Sources

  • The Lens - Patent Citations Database

• Molecular Biology Databases

  • Saccharomyces Genome Database