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
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
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DOI：
10.1073/pnas.89.20.9554
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发表时间：
1992-10-15
影响因子：
11.1
通讯作者：
MEYER, HE
中科院分区：
文献类型：
--
作者：
HEILMEYER, LMG;SERWE, M;MEYER, HE
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.
