A free terminal carboxylate group is required for PhrA pentapeptide inhibition of RapA phosphatase

被引：10

作者：

Core, LJ ^{[1
]}

Ishikawa, S ^{[1
]}

Perego, M ^{[1
]}

机构：

[1] Scripps Res Inst, Dept Mol & Expt Med, Div Cellular Biol, La Jolla, CA 92037 USA

来源：

PEPTIDES | 2001年 / 22卷 / 10期

关键词：

D O I：

10.1016/S0196-9781(01)00491-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In the Bacillus subtilis phosphorelay signal transduction system for sporulation initiation, signals competing with the differentiation process are interpreted by aspartyl-phosphate phosphatases that specifically dephosphorylate the Spo0F or Spo0A response regulators. The RapA phosphatase. is regulated by the PhrA pentapeptide that directly and specifically inhibits its activity. PhrA specificity for RapA inhibition is dependent upon the amino acid sequence of the peptide. Here we show that the pentapeptide affinity for the phosphatase requires a free carboxylate group at the C-terminal amino acid. A free C-terminal carboxylic acid PhrA pentapeptide inhibits RapA phosphatase activity at a 1: 1 ratio and it is approximately 200 fold more active than a C-terminal arn ide peptide. Therefore, coordination of the terminal carboxylate group appears to be critical for peptide binding to RapA. Published by Elsevier Science Inc.

引用

页码：1549 / 1553

页数：5

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