Coupled ATP and DNA binding of adeno-associated virus Rep40 helicase.

Coupled ATP and DNA binding of adeno-associated virus Rep40 helicase. Research Abstract Details 

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Coupled ATP and DNA binding of adeno-associated virus Rep40 helicase. Abstract Text:

Susan S Dignam,Roy F Collaco,Jacob Bieszczad,Patrick Needham,James P Trempe,John David Dignam,

Adeno-associated virus 2 Rep40 helicase is involved in packaging single-stranded genomic DNA into virions. ATPase activity was stimulated 5-10-fold by DNA, depending upon assay conditions. The concentration dependence of Rep40 ATPase activity in the absence and presence of DNA indicates that the monomer is inactive and that the active enzyme is at least a dimer. Binding to oligonucleotides, examined by fluorescence anisotropy, was positively cooperative and required ATP or ATPgammaS; ADP and AMPPCP did not promote binding. The cooperativity and the nucleotide requirement were also demonstrated by surface plasmon resonance. Although the Rep40 behaves as a monomer in solution, it binds to DNA as an oligomer. The requirement of a nucleotide for DNA binding and the stimulation of ATPase activity by DNA indicate that the two processes are linked. Glutaraldehyde cross-linking generated a species that migrates as a trimer on sodium dodecyl sulfate (SDS) gel electrophoresis; ATPS promoted the formation of this species and higher order oligomers. The predominant cross-linked species was a trimer in the absence of ATPgammaS, regardless of whether duplex or single-stranded DNA was present. In the presence of duplex or single-stranded DNA and ATPgammaS, glutaraldehyde cross-linking generated a species that behaved as a dimer on SDS gel elctrophoresis. Sucrose-gradient velocity sedimentation of Rep40 gave an S20,w of 3 in the absence of ligands or in the presence of a 26 bp duplex DNA. The S20,w was 3.5 in the presence of ATPgammaS and 7 and 7.6 in the presence of DNA and ATPgammaS.

Coupled ATP and DNA binding of adeno-associated virus Rep40 helicase. Publishing Authors By Initials

SS Dignam,RF Collaco,J Bieszczad,P Needham,JP Trempe,JD Dignam,

For similar biological phenomena, cell phenomena, and immunity: biological phenomena: microbiologic phenomena: viral physiology: virus replication: virus assembly research abstracts see: biological phenomena, cell phenomena, and immunity: biological phenomena: microbiologic phenomena: viral physiology: virus replication: virus assembly research

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MEDLINE DATE:

Coupled ATP and DNA binding of adeno-associated virus Rep40 helicase. Journal Published:

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

Journal: Biochemistry

VOLUME: 46

Page Numbers: 568-76

Journal Abbreviation: Biochemistry

ISSN: 0006-2960

DAY: 16

MONTH: Jan

YEAR: 2007

Coupled ATP and DNA binding of adeno-associated virus Rep40 helicase. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370623

Coupled ATP and DNA binding of adeno-associated virus Rep40 helicase. Keywords Mesh Terms:

KEYWORDS: Virus Assembly

MESH TERMS: metabolism

Chemical & Substance for Abstract: Coupled ATP and DNA binding of adeno-associated virus Rep40 helicase. Information

Substance Name: Rep40 protein, adeno-associated virus

Registry Number: EC 5.99.-

Grant and Affiliation Information for Coupled ATP and DNA binding of adeno-associated virus Rep40 helicase.

AFFILIATION: Department of Biochemistry and Cancer Biology, University of Toledo College of Medicine, 3035 Arlington Avenue, Toledo, Ohio 43614-5804, USA.

Country: United States

AGENCY: United States PHS

GRANT: PAR-02-036

ACRONYM: GM

MEDLINETA: Biochemistry

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