Document Detail


Single-molecule and bulk approaches to the DnaB replication fork helicase.
MedLine Citation:
PMID:  23276919     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Daniel L Kaplan; Omar A Saleh; Noah Ribeck
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review     Date:  2013-01-01
Journal Detail:
Title:  Frontiers in bioscience (Landmark edition)     Volume:  18     ISSN:  1093-4715     ISO Abbreviation:  Front Biosci (Landmark Ed)     Publication Date:  2013  
Date Detail:
Created Date:  2013-01-01     Completed Date:  2013-06-12     Revised Date:  2013-07-29    
Medline Journal Info:
Nlm Unique ID:  101612996     Medline TA:  Front Biosci (Landmark Ed)     Country:  United States    
Other Details:
Languages:  eng     Pagination:  224-40     Citation Subset:  IM    
Affiliation:
Vanderbilt University, Department of Biological Sciences, Nashville, TN 37235, USA. Daniel.Kaplan@Vanderbilt.Edu
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MeSH Terms
Descriptor/Qualifier:
DNA, Single-Stranded / metabolism*
DnaB Helicases / metabolism*
Fluorescence Resonance Energy Transfer
Magnetics / instrumentation
Models, Molecular
Molecular Motor Proteins / metabolism*
Chemical
Reg. No./Substance:
0/DNA, Single-Stranded; 0/Molecular Motor Proteins; EC 3.1.-/DnaB Helicases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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