Single-molecule and bulk approaches to the DnaB replication fork helicase

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Review

Daniel L. Kaplan^1,*, Omar A. Saleh², Noah Ribeck³

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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

Front. Biosci. (Landmark Ed) 2013, 18(1), 224–240; https://doi.org/10.2741/4097

Published: 1 January 2013

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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.

Keywords

Motor proteins

Helicases

DnaB

Single- Molecule

Branch-Migration

Review

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