Source:http://linkedlifedata.com/resource/pubmed/id/20877334
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
22
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pubmed:dateCreated |
2010-11-18
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pubmed:abstractText |
Escherichia coli UvrD is a 3'-5' superfamily 1A helicase/translocase involved in a variety of DNA metabolic processes. UvrD can function either as a helicase or only as an single-stranded DNA (ssDNA) translocase. The switch between these activities is controlled in vitro by the UvrD oligomeric state; a monomer has ssDNA translocase activity, whereas at least a dimer is needed for helicase activity. Although a 3'-ssDNA partial duplex provides a high-affinity site for a UvrD monomer, here we show that a monomer also binds with specificity to DNA junctions possessing a 5'-ssDNA flanking region and can initiate translocation from this site. Thus, a 5'-ss-duplex DNA junction can serve as a high-affinity loading site for the monomeric UvrD translocase, whereas a 3'-ss-duplex DNA junction inhibits both translocase and helicase activity of the UvrD monomer. Furthermore, the 2B subdomain of UvrD is important for this junction specificity. This highlights a separation of helicase and translocase function for UvrD and suggests that a monomeric UvrD translocase can be loaded at a 5'-ssDNA junction when translocation activity alone is needed.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Single-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/UvrD protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/pcrA protein, Bacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1460-2075
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
17
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pubmed:volume |
29
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3826-39
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pubmed:dateRevised |
2011-1-13
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pubmed:meshHeading |
pubmed-meshheading:20877334-5' Flanking Region,
pubmed-meshheading:20877334-Amino Acid Sequence,
pubmed-meshheading:20877334-Bacterial Proteins,
pubmed-meshheading:20877334-Binding Sites,
pubmed-meshheading:20877334-DNA, Bacterial,
pubmed-meshheading:20877334-DNA, Single-Stranded,
pubmed-meshheading:20877334-DNA Helicases,
pubmed-meshheading:20877334-Escherichia coli,
pubmed-meshheading:20877334-Escherichia coli Proteins,
pubmed-meshheading:20877334-Models, Molecular,
pubmed-meshheading:20877334-Mutation,
pubmed-meshheading:20877334-Protein Binding,
pubmed-meshheading:20877334-Protein Structure, Tertiary,
pubmed-meshheading:20877334-Substrate Specificity
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pubmed:year |
2010
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pubmed:articleTitle |
5'-Single-stranded/duplex DNA junctions are loading sites for E. coli UvrD translocase.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St Louis, MO 63110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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