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PMID: 8289344 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Helix-destabilizing properties of the adenovirus DNA-binding protein.

Journal of virology ·Vol. 68 ·No. 2 ·1994-02-00 ·Pages 1158-64

Zijderveld DC, van der Vliet PC

Abstract

The adenovirus DNA-binding protein (DBP) is a multifunctional protein that is essential for viral DNA replication. DBP binds both single-stranded and double-stranded DNA as well as RNA in a sequence-independent manner. Previous studies showed that DBP does not promote melting of duplex poly(dA-dT) in contrast to prokaryotic single-strand-binding proteins. However, here we show that DBP can displace oligonucleotides annealed to single-stranded M13 DNA. Depending upon the DBP concentration, strands of at least 200 nucleotides can be unwound. Although unwinding of short (17-bp), fully duplex DNA is facilitated by DBP, unwinding of larger (28-bp) duplexes is only possible if single-stranded protruding ends are present. These protruding ends must be at least 4 nucleotides long for optimal unwinding, and both 5' and 3' single-stranded overhangs suffice. DBP-promoted strand displacement is sensitive to MgCl2 and NaCl and not dependent upon ATP. Our results suggest that DBP, through formation of a protein chain on the displaced strand, may destabilize duplex DNA ahead of the replication fork, thereby assisting in strand displacement during replication.

MeSH Terms
Adenoviridae/enzymology Adenovirus E2 Proteins/metabolism DNA Helicases/metabolism DNA-Binding Proteins/metabolism Magnesium Chloride/pharmacology Models, Biological Nucleic Acid Conformation/drug effects Oligonucleotides/metabolism Sodium Chloride/pharmacology
Chemicals
Adenovirus E2 Proteins DNA-Binding Proteins Oligonucleotides Magnesium Chloride Sodium Chloride DNA Helicases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Zijderveld D C
Laboratory for Physiological Chemistry, University of Utrecht, The Netherlands.
van der Vliet P C
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.68.2.1158-1164.1994
Published
1994-02-00
Pages
1158-64
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC236554
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.68.2.1158-1164.1994 PMC Full Text View journal details
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