A conserved regulatory module at the C-terminus of the papillomavirus E1 helicase domain controls E1 helicase assembly

Schuck, S., Stenlund, A. (January 2015) A conserved regulatory module at the C-terminus of the papillomavirus E1 helicase domain controls E1 helicase assembly. Journal of Virology, 89 (2). pp. 1129-1142. ISSN 0022-538x

URL: http://www.ncbi.nlm.nih.gov/pubmed/25378487
DOI: 10.1128/jvi.01903-14

Abstract

Viruses frequently combine multiple activities into one polypeptide to conserve coding capacity. This strategy creates regulatory challenges to ascertain that the combined activities are compatible and do not interfere with each other. The papillomavirus E1 protein, as many other helicases, has the intrinsic ability to form hexamers and double hexamers (DH) that serve as the replicative DNA helicase. However, E1 also has the more unusual ability to generate local melting by forming a double trimer (DT) complex that can untwist the double stranded ori DNA in preparation for DH formation. Here we describe a switching mechanism that allows the papillomavirus E1 protein to form these two different kinds of oligomers and to transition between them. We show that a conserved regulatory module attached to the E1 helicase domain blocks hexamer and DH formation and promotes DT formation. In the presence of the appropriate trigger, the inhibitory effect of the regulatory module is relieved and the transition to DH formation can occur. IMPORTANCE: This study provides a mechanistic understanding into how a multi-functional viral polypeptide can provide different, seemingly incompatible activities. A conserved regulatory sequence module attached to the AAA+ helicase domain in the papillomavirus E1 protein allows the formation of different oligomers with different biochemical activities.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > RNA regulation
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > helicase
organism description > virus
CSHL Authors:
Communities: CSHL Cancer Center Shared Resources > Proteomics Service
CSHL labs > Stenlund lab
CSHL Cancer Center Program > Gene Regulation and Cell Proliferation
Depositing User: Matt Covey
Date: January 2015
Date Deposited: 14 Nov 2014 17:56
Last Modified: 13 Oct 2015 16:20
PMCID: PMC4300631
Related URLs:
URI: http://repository.cshl.edu/id/eprint/30913

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