Bacillus subtilis bacteriophage SPP1 hexameric DNA helicase, G40P, interacts with forked DNA.

Details

Ressource 1Download: serval:BIB_B64DEE343A81.P001 (802.67 [Ko])
State: Public
Version: author
License: Not specified
It was possible to publish this article open access thanks to a Swiss National Licence with the publisher.
Serval ID
serval:BIB_B64DEE343A81
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Bacillus subtilis bacteriophage SPP1 hexameric DNA helicase, G40P, interacts with forked DNA.
Journal
Nucleic Acids Research
Author(s)
Ayora S., Weise F., Mesa P., Stasiak A., Alonso J.C.
ISSN
1362-4962[electronic], 0305-1048[linking]
Publication state
Published
Issued date
06/2002
Volume
30
Number
11
Pages
2280-2289
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Abstract
SPP1-encoded replicative DNA helicase gene 40 product (G40P) is an essential product for phage replication. Hexameric G40P, in the presence of AMP-PNP, preferentially binds unstructured single-stranded (ss)DNA in a sequence-independent manner. The efficiency of ssDNA binding, nucleotide hydrolysis and the unwinding activity of G40P are affected in a different manner by different nucleotide cofactors. Nuclease protection studies suggest that G40P protects the 5' tail of a forked molecule, and the duplex region at the junction against exonuclease attack. G40P does not protect the 3' tail of a forked molecule from exonuclease attack. By using electron microscopy we confirm that the ssDNA transverses the centre of the hexameric ring. Our results show that hexameric G40P DNA helicase encircles the 5' tail, interacts with the duplex DNA at the ss-double-stranded DNA junction and excludes the 3' tail of the forked DNA.
Keywords
Adenosine Triphosphatases/chemistry, Adenosine Triphosphatases/metabolism, Bacillus subtilis/virology, Bacteriophages/enzymology, DNA/chemistry, DNA/genetics, DNA Footprinting, DNA Helicases/chemistry, DNA Helicases/metabolism, DNA, Single-Stranded/chemistry, DNA, Single-Stranded/genetics, DNA, Viral/chemistry, DNA, Viral/genetics, DNA-Binding Proteins/chemistry, DNA-Binding Proteins/metabolism, Hydrolysis, Microscopy, Electron, Models, Biological, Nucleic Acid Conformation, Protein Binding, Viral Proteins/chemistry, Viral Proteins/metabolism
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 10:36
Last modification date
25/09/2019 6:10
Usage data