A function for the psi subunit in loading the Escherichia coli DNA polymerase sliding clamp.

A function for the psi subunit in loading the Escherichia coli DNA polymerase sliding clamp. Research Abstract Details 

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A function for the psi subunit in loading the Escherichia coli DNA polymerase sliding clamp. Abstract Text:

Stephen G Anderson,Christopher R Williams,Mike O'donnell,Linda B Bloom,

Crystal structures of an Escherichia coli clamp loader have provided insight into the mechanism by which this molecular machine assembles ring-shaped sliding clamps onto DNA. The contributions made to the clamp loading reaction by two subunits, chi and psi, which are not present in the crystal structures, were determined by measuring the activities of three forms of the clamp loader, gamma(3)deltadelta', gamma(3)deltadelta'psi, and gamma(3)deltadelta'psichi. The psi subunit is important for stabilizing an ATP-induced conformational state with high affinity for DNA, whereas the chi subunit does not contribute directly to clamp loading in our assays lacking single-stranded DNA-binding protein. The psi subunit also increases the affinity of the clamp loader for the clamp in assays in which ATPgammaS is substituted for ATP. Interestingly, the affinity of the gamma(3)deltadelta' complex for beta is no greater in the presence than in the absence of ATPgammaS. A role for psi in stabilizing or promoting ATP- and ATPgammaS-induced conformational changes may explain why large conformational differences were not seen in gamma(3)deltadelta' structures with and without bound ATPgammaS. The beta clamp partially compensates for the activity of psi when this subunit is not present and possibly serves as a scaffold on which the clamp loader adopts the appropriate conformation for DNA binding and clamp loading. Results from our work and others suggest that the psi subunit may introduce a temporal order to the clamp loading reaction in which clamp binding precedes DNA binding.

A function for the psi subunit in loading the Escherichia coli DNA polymerase sliding clamp. Publishing Authors By Initials

SG Anderson,CR Williams,M O'donnell,LB Bloom,

For similar proteins: protein subunits research abstracts see: proteins: protein subunits research

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A function for the psi subunit in loading the Escherichia coli DNA polymerase sliding clamp. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 7035-45

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 8

MONTH: 01

YEAR: 2007

A function for the psi subunit in loading the Escherichia coli DNA polymerase sliding clamp. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

A function for the psi subunit in loading the Escherichia coli DNA polymerase sliding clamp. Keywords Mesh Terms:

KEYWORDS: Protein Subunits

MESH TERMS: physiology

Chemical & Substance for Abstract: A function for the psi subunit in loading the Escherichia coli DNA polymerase sliding clamp. Information

Substance Name: Adenosine Triphosphatases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for A function for the psi subunit in loading the Escherichia coli DNA polymerase sliding clamp.

AFFILIATION: Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, Florida 32610-0245, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM38839

ACRONYM: GM

MEDLINETA: J Biol Chem

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