Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 7-Day Trial for You or Your Team.

Learn More →

Motors and switches: AAA+ machines within the replisome

Motors and switches: AAA+ machines within the replisome The Escherichia coli clamp loader, γ-complex, loads the ring-shaped β-clamp onto DNA in an ATP driven reaction in which the clamp is cracked open, brought to a primed site and closed around the DNA. AAA+ (ATPases associated with a variety of cellular activities) proteins are involved in many different aspects of DNA metabolism. The γ- and δ′-subunits of the γ-complex are AAA+ proteins and so are clamp-loader subunits from eukaryotes, archaea and T4 bacteriophage. The recent crystal structure of the γ3δδ′-assembly, an active clamp loader, indicates that the clamp loader is a pentameric ring. A striking feature of this assembly is the location of ATP sites at the interfaces of the subunits. Clamp loaders from eukaryotes, archaea and T4 bacteriophage share similarities to the E. coli γ-complex and models similar to that of of the E. coli γ-complex can be made for each of these clamp loaders. Many other replication proteins are AAA+ proteins, including the replication initiation proteins, DnaA, the origin recognition complex (ORC), Mcm2–7, Cdc6 and DnaC. The similarities between the γ-complex subunits and other AAA+ proteins that are involved in replication initiation, lead to a model for the function of the replication-initiation proteins based on γ-complex structural and biochemical data. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Reviews Molecular Cell Biology Springer Journals

Motors and switches: AAA+ machines within the replisome

Loading next page...
 
/lp/springer-journals/motors-and-switches-aaa-machines-within-the-replisome-7FOVce48lq

References (108)

Publisher
Springer Journals
Copyright
Copyright © 2002 by Nature Publishing Group
Subject
Life Sciences; Life Sciences, general; Cell Biology; Cancer Research; Developmental Biology; Stem Cells; Biochemistry, general
ISSN
1471-0072
eISSN
1471-0080
DOI
10.1038/nrm949
Publisher site
See Article on Publisher Site

Abstract

The Escherichia coli clamp loader, γ-complex, loads the ring-shaped β-clamp onto DNA in an ATP driven reaction in which the clamp is cracked open, brought to a primed site and closed around the DNA. AAA+ (ATPases associated with a variety of cellular activities) proteins are involved in many different aspects of DNA metabolism. The γ- and δ′-subunits of the γ-complex are AAA+ proteins and so are clamp-loader subunits from eukaryotes, archaea and T4 bacteriophage. The recent crystal structure of the γ3δδ′-assembly, an active clamp loader, indicates that the clamp loader is a pentameric ring. A striking feature of this assembly is the location of ATP sites at the interfaces of the subunits. Clamp loaders from eukaryotes, archaea and T4 bacteriophage share similarities to the E. coli γ-complex and models similar to that of of the E. coli γ-complex can be made for each of these clamp loaders. Many other replication proteins are AAA+ proteins, including the replication initiation proteins, DnaA, the origin recognition complex (ORC), Mcm2–7, Cdc6 and DnaC. The similarities between the γ-complex subunits and other AAA+ proteins that are involved in replication initiation, lead to a model for the function of the replication-initiation proteins based on γ-complex structural and biochemical data.

Journal

Nature Reviews Molecular Cell BiologySpringer Journals

Published: Nov 1, 2002

There are no references for this article.