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Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals.

Abstract：

:ClpXP is a protease involved in DNA damage repair, stationary-phase gene expression, and ssrA-mediated protein quality control. To date, however, only a handful of ClpXP substrates have been identified. Using a tagged and inactive variant of ClpP, substrates of E. coli ClpXP were trapped in vivo, purified, and identified by mass spectrometry. The more than 50 trapped proteins include transcription factors, metabolic enzymes, and proteins involved in the starvation and oxidative stress responses. Analysis of the sequences of the trapped proteins revealed five recurring motifs: two located at the C terminus of proteins, and three N-terminal motifs. Deletion analysis, fusion proteins, and point mutations established that sequences from each motif class targeted proteins for degradation by ClpXP. These results represent a description of general rules governing substrate recognition by a AAA+ family ATPase and suggest strategies for regulation of protein degradation.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Flynn JM,Neher SB,Kim YI,Sauer RT,Baker TA

doi

10.1016/s1097-2765(03)00060-1

subject

Has Abstract

pub_date

2003-03-01 00:00:00

pages

671-83

issue

3

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(03)00060-1

journal_volume

11

pub_type

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