FARNESYLCYSTEINE, A CONSTITUENT OF THE ALPHA AND BETA SUBUNITS OF RABBIT SKELETAL-MUSCLE PHOSPHORYLASE-KINASE - LOCALIZATION BY CONVERSION TO S-ETHYLCYSTEINE AND BY TANDEM MASS-SPECTROMETRY

被引：51

作者：

HEILMEYER, LMG ^{[1
]}

SERWE, M ^{[1
]}

WEBER, C ^{[1
]}

METZGER, J ^{[1
]}

HOFFMANNPOSORSKE, E ^{[1
]}

MEYER, HE ^{[1
]}

机构：

[1] UNIV TUBINGEN, INST ORGAN CHEM, W-7400 TUBINGEN 1, GERMANY

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1992年 / 89卷 / 20期

关键词：

D O I：

10.1073/pnas.89.20.9554

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The primary structure of the alpha and beta subunits of phosphorylase kinase reveals that both proteins contain a carboxyl-terminal CA1A2X motif (where C is cysteine, A1 and A2 are aliphatic amino acids, and X is an uncharged amino acid), the recognition signal for a protein polyisoprenyltransferase. The product, a polyisoprenylated cysteine, can be detected by phenylthiocarbamoylamino acid analysis and by microsequencing following conversion to S-ethylcysteine. Mass spectrometry confirms a covalently linked farnesyl residue in both subunits. Tandem mass spectrometry localizes these modifications at the cysteine residues present in the carboxyl-terminal CAMQ and CLVS sequences of the alpha and beta subunits, respectively. Membrane association of phosphorylase kinase, probably mediated by these farnesyl residues, is discussed.

引用

页码：9554 / 9558

页数：5

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