Open Access
Review
Single-molecule and bulk approaches to the DnaB replication fork helicase
Daniel L. Kaplan1,*,Omar A. Saleh2,Noah Ribeck3
1
Department of Biological Sciences, Vanderbilt University, VU Station B, Box 35-1634, Nashville TN 37235, USA
2
Materials Dept., University of California, Santa Barbara CA 93106, USA
3
Department of Microbiology and Molecular Genetics, Michigan State University, 2215 Biomedical Physical Sciences, East Lansing MI 48824, USA
DOI: 10.2741/4097 Volume 18 Issue 1, pp.224-240
Published: 01 January 2013
(This article belongs to the Special Issue DNA motor proteins - biochemical and biophysical studies)
*Corresponding Author(s):  
Daniel L. Kaplan
E-mail:  
Daniel.Kaplan@Vanderbilt.Edu
Abstract

Motor proteins are enzymes that accomplish mechanical work in a wide variety of biological processes. In this review we focus on bulk and single molecule methods to study how motor proteins function. We discuss in detail the analysis of the motor protein DnaB, a hexameric helicase that unwinds DNA at a replication fork in Gram-negative bacteria. Bulk and single-molecule studies have complemented one another to arrive at a comprehensive mechanistic view of how DnaB unwinds double-stranded DNA.

Key words

Motor proteins, Helicases, DnaB, Single- Molecule, Branch-Migration, Review

Share and Cite
Daniel L. Kaplan, Omar A. Saleh, Noah Ribeck. Single-molecule and bulk approaches to the DnaB replication fork helicase. Frontiers in Bioscience-Landmark. 2013. 18(1); 224-240.