Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C.

Abstract:

:The heptapeptide-nucleotide microcin C (McC) targets aspartyl-tRNA synthetase. Upon its entry into a susceptible cell, McC is processed to release a nonhydrolyzable aspartyl-adenylate that inhibits aspartyl-tRNA synthetase, leading to the cessation of translation and cell growth. Here, we surveyed Escherichia coli cells with singly, doubly, and triply disrupted broad-specificity peptidase genes to show that any of three nonspecific oligopeptidases (PepA, PepB, or PepN) can effectively process McC. We also show that the rate-limiting step of McC processing in vitro is deformylation of the first methionine residue of McC.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Kazakov T,Vondenhoff GH,Datsenko KA,Novikova M,Metlitskaya A,Wanner BL,Severinov K

doi

10.1128/JB.01956-07

subject

Has Abstract

pub_date

2008-04-01 00:00:00

pages

2607-10

issue

7

eissn

0021-9193

issn

1098-5530

pii

JB.01956-07

journal_volume

190

pub_type

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