Solution structure of an “open” E. coli Pol III clamp loader sliding clamp complex

Sliding clamps are opened and loaded onto primer template junctions by clamp loaders, and once loaded on DNA, confer processivity to replicative polymerases. Previously determined crystal structures of eukaryotic and T4 clamp loader-clamp complexes have captured the sliding clamps in either closed o...

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Bibliographic Details
Published in:Journal of structural biology 2016-06, Vol.194 (3), p.272-281
Main Authors: Tondnevis, Farzaneh, Weiss, Thomas M., Matsui, Tsutomu, Bloom, Linda B., McKenna, Robert
Format: Article
Language:English
Subjects:
AAA+ ATPase
Adenosine Triphosphate - metabolism
Binding Sites
Chromatography, Gel
Clamp loader
DNA Polymerase III - metabolism
DNA Replication
DNA, Bacterial
DNA-Directed DNA Polymerase
Escherichia coli - enzymology
Escherichia coli - genetics
Escherichia coli Proteins
Models, Molecular
Protein Conformation
Protein Subunits
SAXS
Scattering, Small Angle
Sliding clamp
Solutions
X-Ray Diffraction
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Summary:Sliding clamps are opened and loaded onto primer template junctions by clamp loaders, and once loaded on DNA, confer processivity to replicative polymerases. Previously determined crystal structures of eukaryotic and T4 clamp loader-clamp complexes have captured the sliding clamps in either closed or only partially open interface conformations. In these solution structure studies, we have captured for the first time the clamp loader-sliding clamp complex from Escherichia coli using size exclusion chromatography coupled to small angle X-ray scattering (SEC-SAXS). The data suggests the sliding clamp is in an open conformation which is wide enough to permit duplex DNA binding. The data also provides information about spatial arrangement of the sliding clamp with respect to the clamp loader subunits and is compared to complex crystal structures determined from other organisms.
ISSN:1047-8477
1095-8657
DOI:10.1016/j.jsb.2016.03.003