法尼基转移酶β亚基中的底物特异性决定因素。
Substrate specificity determinants in the farnesyltransferase beta-subunit.
作者信息
Trueblood C E, Boyartchuk V L, Rine J
机构信息
Division of Genetics, Department of Molecular and Cell Biology, 401 Barker Hall, University of California, Berkeley, CA 94720, USA.
出版信息
Proc Natl Acad Sci U S A. 1997 Sep 30;94(20):10774-9. doi: 10.1073/pnas.94.20.10774.
Protein prenyltransferases catalyze the covalent attachment of isoprenoid lipids (farnesyl or geranylgeranyl) to a cysteine near the C terminus of their substrates. This study explored the specificity determinants for interactions between the farnesyltransferase of Saccharomyces cerevisiae and its protein substrates. A series of substitutions at amino acid 149 of the farnesyltransferase beta-subunit were tested in combination with a series of substitutions at the C-terminal amino acid of CaaX protein substrates Ras2p and a-factor. Efficient prenylation was observed when oppositely charged amino acids were present at amino acid 149 of the yeast farnesyltransferase beta-subunit and the C-terminal amino acid of the CaaX protein substrate, but not when like charges were present at these positions. This evidence for electrostatic interaction between amino acid 149 and the C-terminal amino acid of CaaX protein substrates leads to the prediction that the C-terminal amino acid of the protein substrate binds near amino acid 149 of the yeast farnesyltransferase beta-subunit.
蛋白质异戊二烯基转移酶催化类异戊二烯脂质（法尼基或香叶基香叶基）与底物C末端附近的半胱氨酸共价连接。本研究探讨了酿酒酵母法尼基转移酶与其蛋白质底物之间相互作用的特异性决定因素。对法尼基转移酶β亚基第149位氨基酸进行了一系列取代，并与CaaX蛋白底物Ras2p和α因子的C末端氨基酸的一系列取代相结合进行测试。当酵母法尼基转移酶β亚基的第149位氨基酸和CaaX蛋白底物的C末端氨基酸存在相反电荷的氨基酸时，观察到高效的异戊二烯基化，而当这些位置存在相同电荷时则未观察到。第149位氨基酸与CaaX蛋白底物C末端氨基酸之间存在静电相互作用的证据表明，蛋白质底物的C末端氨基酸结合在酵母法尼基转移酶β亚基第149位氨基酸附近。
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