RAS2 protein of Saccharomyces cerevisiae is methyl-esterified at its carboxyl terminus

R. J. Deschenes, J. B. Stimmel, S. Clarke, J. Stock, James Broach

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

Yeast and mammalian RAS gene products are GTP-binding proteins that are posttranslationally localized to the inner surface of the plasma membrane. This localization is accomplished by the addition of a lipid moiety to a conserved cysteine residue close to the carboxyl terminus. In a previous report we showed that the mammalian Ha-ras protein is also modified posttranslationally by methyl esterification. Here we show that the yeast RAS2 protein is posttranslationally modified by methyl esterification at or near the carboxyl terminus. We also present evidence indicating that the methyl ester is linked to the conserved cysteine residue, implying that RAS2 protein is cleaved to expose this cysteine as the carboxyl-terminal residue. This maturation pathway may be shared by a family of proteins that are initially synthesized as soluble proteins and must become membrane-localized to function.

Original languageEnglish (US)
Pages (from-to)11865-11873
Number of pages9
JournalJournal of Biological Chemistry
Volume264
Issue number20
StatePublished - 1989

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Saccharomyces cerevisiae Proteins
Cysteine
Esterification
ras Proteins
Proteins
Fungal Proteins
Cell membranes
GTP-Binding Proteins
Yeast
Esters
Genes
Yeasts
Cell Membrane
Membranes
Lipids

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Medicine(all)
  • Molecular Biology
  • Cell Biology

Cite this

Deschenes, R. J., Stimmel, J. B., Clarke, S., Stock, J., & Broach, J. (1989). RAS2 protein of Saccharomyces cerevisiae is methyl-esterified at its carboxyl terminus. Journal of Biological Chemistry, 264(20), 11865-11873.
Deschenes, R. J. ; Stimmel, J. B. ; Clarke, S. ; Stock, J. ; Broach, James. / RAS2 protein of Saccharomyces cerevisiae is methyl-esterified at its carboxyl terminus. In: Journal of Biological Chemistry. 1989 ; Vol. 264, No. 20. pp. 11865-11873.
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Deschenes, RJ, Stimmel, JB, Clarke, S, Stock, J & Broach, J 1989, 'RAS2 protein of Saccharomyces cerevisiae is methyl-esterified at its carboxyl terminus', Journal of Biological Chemistry, vol. 264, no. 20, pp. 11865-11873.

RAS2 protein of Saccharomyces cerevisiae is methyl-esterified at its carboxyl terminus. / Deschenes, R. J.; Stimmel, J. B.; Clarke, S.; Stock, J.; Broach, James.

In: Journal of Biological Chemistry, Vol. 264, No. 20, 1989, p. 11865-11873.

Research output: Contribution to journalArticle

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T1 - RAS2 protein of Saccharomyces cerevisiae is methyl-esterified at its carboxyl terminus

AU - Deschenes, R. J.

AU - Stimmel, J. B.

AU - Clarke, S.

AU - Stock, J.

AU - Broach, James

PY - 1989

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AB - Yeast and mammalian RAS gene products are GTP-binding proteins that are posttranslationally localized to the inner surface of the plasma membrane. This localization is accomplished by the addition of a lipid moiety to a conserved cysteine residue close to the carboxyl terminus. In a previous report we showed that the mammalian Ha-ras protein is also modified posttranslationally by methyl esterification. Here we show that the yeast RAS2 protein is posttranslationally modified by methyl esterification at or near the carboxyl terminus. We also present evidence indicating that the methyl ester is linked to the conserved cysteine residue, implying that RAS2 protein is cleaved to expose this cysteine as the carboxyl-terminal residue. This maturation pathway may be shared by a family of proteins that are initially synthesized as soluble proteins and must become membrane-localized to function.

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