Assembly of a double hexameric helicase

Schuck, S., Stenlund, A. (November 2005) Assembly of a double hexameric helicase. Mol Cell, 20 (3). pp. 377-89. ISSN 1097-2765 (Print)

URL: http://www.ncbi.nlm.nih.gov/pubmed/16285920
DOI: 10.1016/j.molcel.2005.09.020

Abstract

Viral initiators perform multiple functions in initiation of DNA replication including ori binding, melting, and unwinding, culminating in the formation of a double hexameric (DH) helicase. We have recapitulated the assembly of the papillomavirus E1 initiator DH helicase, providing the first description of how such a complex is formed. We have identified an intermediate, a double trimer (DT), which relies on two cooperating DNA binding activities to melt double-stranded DNA and generate a substrate for formation of the DH helicase. The formation of the DT is dependent on nucleotide binding, while formation of the DH also requires hydrolysable ATP. The DNA binding properties of the DT explain how E1, which binds to DNA as a dimer, can effect a transition to ring structures, such as the double hexamer. These results provide new insight into the intricate machinery that initiates DNA replication.

Item Type: Paper
Uncontrolled Keywords: Adenosine Triphosphate metabolism DNA Helicases chemistry genetics metabolism DNA Replication physiology DNA Viral metabolism Papillomaviridae chemistry genetics metabolism Protein Structure Quaternary physiology Viral Proteins chemistry genetics metabolism
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > DNA replication
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > helicase
organism description > virus > papillomavirus
CSHL Authors:
Communities: CSHL labs > Stenlund lab
Depositing User: Brian Soldo
Date: 11 November 2005
Date Deposited: 15 Mar 2012 14:07
Last Modified: 01 Mar 2013 20:33
Related URLs:
URI: http://repository.cshl.edu/id/eprint/25180

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