Analyses of the interaction between the origin binding domain from simian virus 40 T antigen and single-stranded DNA provide insights into DNA unwinding and initiation of DNA replication.

Analyses of the interaction between the origin binding domain from simian virus 40 T antigen and single-stranded DNA provide insights into DNA unwinding and initiation of DNA replication. Research Abstract Details 

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Analyses of the interaction between the origin binding domain from simian virus 40 T antigen and single-stranded DNA provide insights into DNA unwinding and initiation of DNA replication. Abstract Text:

Danielle K Reese,Gretchen Meinke,Anuradha Kumar,Stephanie Moine,Kathleen Chen,James L Sudmeier,William Bachovchin,Andrew Bohm,Peter A Bullock,

DNA helicases are essential for DNA metabolism; however, at the molecular level little is known about how they assemble or function. Therefore, as a model for a eukaryotic helicase, we are analyzing T antigen (T-ag) the helicase encoded by simian virus 40. In this study, nuclear magnetic resonance (NMR) methods were used to investigate the transit of single-stranded DNA (ssDNA) through the T-ag origin-binding domain (T-ag OBD). When the residues that interact with ssDNA are viewed in terms of the structure of a hexamer of the T-ag OBD, comprised of residues 131 to 260, they indicate that ssDNA passes over one face of the T-ag OBD and then transits through a gap in the open ring structure. The NMR-based conclusions are supported by an analysis of previously described mutations that disrupt critical steps during the initiation of DNA replication. These and related observations are discussed in terms of the threading of DNA through T-ag hexamers and the initiation of viral DNA replication.

Analyses of the interaction between the origin binding domain from simian virus 40 T antigen and single-stranded DNA provide insights into DNA unwinding and initiation of DNA replication. Publishing Authors By Initials

DK Reese,G Meinke,A Kumar,S Moine,K Chen,JL Sudmeier,W Bachovchin,A Bohm,PA Bullock,

For similar viruses: dna viruses: polyomaviridae: polyomavirus: simian virus 40 research abstracts see: viruses: dna viruses: polyomaviridae: polyomavirus: simian virus 40 research

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Analyses of the interaction between the origin binding domain from simian virus 40 T antigen and single-stranded DNA provide insights into DNA unwinding and initiation of DNA replication. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of virology

VOLUME: 80

Page Numbers: 12248-59

Journal Abbreviation: J. Virol.

ISSN: 0022-538X

DAY: 27

MONTH: 09

YEAR: 2006

Analyses of the interaction between the origin binding domain from simian virus 40 T antigen and single-stranded DNA provide insights into DNA unwinding and initiation of DNA replication. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 113724

Analyses of the interaction between the origin binding domain from simian virus 40 T antigen and single-stranded DNA provide insights into DNA unwinding and initiation of DNA replication. Keywords Mesh Terms:

KEYWORDS: Simian virus 40

MESH TERMS: genetics

Chemical & Substance for Abstract: Analyses of the interaction between the origin binding domain from simian virus 40 T antigen and single-stranded DNA provide insights into DNA unwinding and initiation of DNA replication. Information

Substance Name: DNA Helicases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for Analyses of the interaction between the origin binding domain from simian virus 40 T antigen and single-stranded DNA provide insights into DNA unwinding and initiation of DNA replication.

AFFILIATION: Department of Biochemistry A703, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: 9R01GM55397

ACRONYM: GM

MEDLINETA: J Virol

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