Quantitative Analysis of Binding of Single-Stranded DNA by Escherichia coli DnaB Helicase and the DnaB·DnaC Complex-Reference-Cited by-同舟云学术

Quantitative Analysis of Binding of Single-Stranded DNA by Escherichia coli DnaB Helicase and the DnaB·DnaC Complex

Published:2006-08-31 Issue:38 Volume:45 Page:11505-11513
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Biswas Subhasis B.¹,Biswas-Fiss Esther E.¹

Affiliation:

1. Department of Molecular Biology, School of Medicine and Graduate School of Biomedical Sciences, University of Medicine and Dentistry of New Jersey, Stratford, New Jersey 08084, and Program in Biotechnology, Department of Bioscience Technologies, Thomas Jefferson University, Philadelphia, Pennsylvania 19107

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi060118d

Reference37 articles.

1. The Escherichia coli dnaB replication protein is a DNA helicase.

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1. Crystal structure of the complex of the interaction domains of Escherichia coli DnaB helicase and DnaC helicase loader: structural basis implying a distortion-accumulation mechanism for the DnaB ring opening caused by DnaC binding;The Journal of Biochemistry;2019-10-30

2. The DnaA AAA+ Domain His136 Residue Directs DnaB Replicative Helicase to the Unwound Region of the Replication Origin, oriC;Frontiers in Microbiology;2018-08-31

3. DnaC, the indispensable companion of DnaB helicase, controls the accessibility of DnaB helicase by primase;Journal of Biological Chemistry;2017-12

4. Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile;Open Biology;2016-12

5. Interactions between helicase and primase are crucial for DNA replication in the enteropathogen Clostridium difficile;2016-08-29