Interactions of the Escherichia coli DnaB−DnaC Protein Complex with Nucleotide Cofactors. 1. Allosteric Conformational Transitions of the Complex-Reference-Cited by-同舟云学术

Interactions of the Escherichia coli DnaB−DnaC Protein Complex with Nucleotide Cofactors. 1. Allosteric Conformational Transitions of the Complex

Published:2009-07-01 Issue:29 Volume:48 Page:6712-6729
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Roychowdhury Anasuya¹,Szymanski Michal R.¹,Jezewska Maria J.¹,Bujalowski Wlodzimierz¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, Department of Obstetrics and Gynecology, and The Sealy Center for Structural Biology and Molecular Biophysics, Sealy Center for Cancer Cell Biology, The University of Texas Medical Branch at Galveston, 301 University Boulevard, Galveston, Texas 77555-1053

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi900050x

Reference60 articles.

1. Coupling of a Replicative Polymerase and Helicase: A τ–DnaB Interaction Mediates Rapid Replication Fork Movement

2. Non-replicative helicases at the replication fork

3. Stoichiometry of DnaA and DnaB Protein in Initiation at the Escherichia coli Chromosomal Origin

4. Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme.

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