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J. Biol. Chem., Vol. 281, Issue 46, 99937, November 17, 2006

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Arginine Fingers Give Clamp Loader a Hand

During DNA replication, DNA polymerase is tethered to DNA via a clamp, which is placed onto the DNA by a clamp loader. In eukaryotes, the pentameric clamp loader known as replication factor C (RFC) uses energy from ATP binding and hydrolysis to recruit a clamp called proliferating cell nuclear antigen (PCNA), break one clamp interface, and topologically link the clamp to primed template DNA. RFC contains four ATP sites with four associated arginine fingers that sense ATP binding and catalyze ATP hydrolysis.

Residues in the central chamber of RFC are required for DNA binding.

In this study, Aaron Johnson and colleagues mutated the arginine fingers on RFC to determine the role of the fingers and their ATP sites in the PCNA loading mechanism. They show that none of the arginine fingers are needed for PCNA interaction and ring opening. However, their results demonstrate that certain ATP sites on RFC play distinct roles downstream of the PCNA opening. For example, the arginine finger in ATP site C is needed for RFC to bind DNA, and ATP hydrolysis in site D is specifically triggered by PCNA. The authors hypothesize that this site D hydrolysis leads to closure of PCNA around DNA.

FOOTNOTES

See referenced article, J. Biol. Chem. 2006, 281, 35531-35543

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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Related Collections Papers Of The Week Social Bookmarking                      What's this?