NDLI: Endoproteolytic processing of a farnesylated peptide in vitro.

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Endoproteolytic processing of a farnesylated peptide in vitro.

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Endoproteolytic processing of a farnesylated peptide in vitro.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Rine, J. Ashby, M. N. King, D. S.
Description	Author Affiliation: Ashby MN ( Department of Molecular and Cell Biology, University of California, Berkeley 94720.);
Abstract	Numerous eukaryotic proteins containing a carboxyl-terminal CAAX motif (C, cysteine; A, aliphatic amino acid; X, any amino acid) require a three-step posttranslational processing for localization and function. The a mating factor of Saccharomyces cerevisiae is one such protein, requiring cysteine farnesylation, proteolysis of the terminal three amino acids, and carboxyl methylation for biological activity. We have used farnesylated a-factor peptides to examine the proteolytic step in the maturation of CAAX-containing proteins. Three distinct carboxyl-terminal protease activities were found in yeast cell extracts that could remove the terminal three residues of a-factor. Two of the proteolytic activities were in cytosolic fractions. One of these activities was a PEP4-dependent carboxypeptidase that was sensitive to phenylmethylsulfonyl fluoride. The other cytosolic activity was PEP4-independent, sensitive to 1,10-phenanthroline, and effectively inhibited by an unfarnesylated a-factor peptide. In contrast, a protease activity in membrane fractions was unaffected by phenylmethylsulfonyl fluoride, 1,10-phenanthroline, or unfarnesylated a-factor peptide. Incubation of membrane preparations from either yeast or rat liver with a radiolabeled farnesylated a-factor peptide released the terminal three amino acids intact as a tripeptide, indicating that this reaction occurred by an endoproteolytic mechanism and that the enzyme most likely possesses a broad substrate specificity. The yeast endoprotease was not significantly affected by a panel of protease inhibitors, suggesting that the enzyme is novel. Zinc ion was shown to inhibit the endoprotease (Ki less than 100 microM). The specific activities of the a-factor carboxyl-terminal membrane endoprotease and methyltransferase clearly indicated that the proteolytic reaction was not rate-limiting in these processing reactions in vitro.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	10
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cysteine Analogs & Derivatives Endopeptidases Metabolism Methyltransferases Peptides Saccharomyces Cerevisiae Enzymology Amino Acid Sequence Cell Membrane Cytosol Isolation & Purification Kinetics Molecular Sequence Data Oligopeptides Chemical Synthesis Pheromones Protein Processing, Post-Translational Substrate Specificity Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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