Inhibition of protein interactions with the beta 2 sliding clamp of Escherichia coli DNA polymerase III by peptides from beta 2-binding proteins.

Abstract:

:The sliding clamp of the Escherichia coli replisome is now understood to interact with many proteins involved in DNA synthesis and repair. A universal interaction motif is proposed to be one mechanism by which those proteins bind the E. coli sliding clamp, a homodimer of the beta subunit, at a single site on the dimer. The numerous beta(2)-binding proteins have various versions of the consensus interaction motif, including a related hexameric sequence. To determine if the variants of the motif could contribute to the competition of the beta-binding proteins for the beta(2) site, synthetic peptides derived from the putative beta(2)-binding motifs were assessed for their abilities to inhibit protein-beta(2) interactions, to bind directly to beta(2), and to inhibit DNA synthesis in vitro. A hierarchy emerged, which was consistent with sequence similarity to the pentameric consensus motif, QL(S/D)LF, and peptides containing proposed hexameric motifs were shown to have activities comparable to those containing the consensus sequence. The hierarchy of peptide binding may be indicative of a competitive hierarchy for the binding of proteins to beta(2) in various stages or circumstances of DNA replication and repair.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Wijffels G,Dalrymple BP,Prosselkov P,Kongsuwan K,Epa VC,Lilley PE,Jergic S,Buchardt J,Brown SE,Alewood PF,Jennings PA,Dixon NE

doi

10.1021/bi036229j

subject

Has Abstract

pub_date

2004-05-18 00:00:00

pages

5661-71

issue

19

eissn

0006-2960

issn

1520-4995

journal_volume

43

pub_type

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