NDLI: A universal protein–protein interaction motif in the eubacterial DNA replication and repair systems

Content Provider	PubMed Central
Author	Dalrymple, Brian P. Kongsuwan, Kritaya Wijffels, Gene Dixon, Nicholas E. Jennings, Philip A.
Copyright Year	2001
Abstract	The interaction between DNA polymerases and sliding clamp proteins confers processivity in DNA synthesis. This interaction is critical for most DNA replication machines from viruses and prokaryotes to higher eukaryotes. The clamp proteins also participate in a variety of dynamic and competing protein–protein interactions. However, clamp-protein binding sequences have not so far been identified in the eubacteria. Here we show from three lines of evidence, bioinformatics, yeast two-hybrid analysis, and inhibition of protein–protein interaction by modified peptides, that variants of a pentapeptide motif (consensus QL[SD]LF) are sufficient to enable interaction of a number of proteins with an archetypal eubacterial sliding clamp (the β subunit of Escherichia coli DNA polymerase III holoenzyme). Representatives of this motif are present in most sequenced members of the eubacterial DnaE, PolC, PolB, DinB, and UmuC families of DNA polymerases and the MutS1 mismatch repair protein family. The component tripeptide DLF inhibits the binding of the α (DnaE) subunit of E. coli DNA polymerase III to β at μM concentration, identifying key residues. Comparison of the eubacterial, eukaryotic, and archaeal sliding clamp binding motifs suggests that the basic interactions have been conserved across the evolutionary landscape.
Related Links	http://dx.doi.org/10.1073/pnas.191384398
Starting Page	11627
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	20
Volume Number	98
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2001-09-25
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems.

Interaction between replication protein A and p53 is disrupted after UV damage in a DNA repair-dependent manner

Replication protein A binds to regulatory elements in yeast DNA repair and DNA metabolism genes.

Interaction between replication protein A and p53 is disrupted after UV damage in a DNA repair-dependent manner.

An interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repair.

Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair.

An interaction between the dna repair factor xpa and replication protein a appears essential for nucleotide excision repair (1995).

DNA annealing by Rad52 Protein is stimulated by specific interaction with the complex of replication protein A and single-stranded DNA

Single-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein A

A universal protein–protein interaction motif in the eubacterial DNA replication and repair systems

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A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems.

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Interaction between replication protein A and p53 is disrupted after UV damage in a DNA repair-dependent manner.

An interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repair.

Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair.

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A universal protein–protein interaction motif in the eubacterial DNA replication and repair systems