Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1991-10-31
pubmed:abstractText
The ruv operon is induced by treatments that damage DNA and is regulated by the LexA repressor. It encodes two proteins, RuvA and RuvB, that are involved in DNA repair, recombination in RecE and RecF pathways, and mutagenesis. RuvB protein was previously purified and has ATP-binding activity and weak ATPase activity. To study the biochemical properties of RuvA and its interaction with RuvB, we purified RuvA protein to near homogeneity from an over-producing strain. RuvA bound more efficiently to single-stranded DNA than to double-stranded DNA. RuvA bound to DNA greatly enhanced the ATPase activity of RuvB; the enhancing effect of various forms of DNA was in the order of supercoiled DNA greater than single-stranded DNA greater than linear double-stranded DNA. UV irradiation further enhanced the ATPase stimulatory effect of supercoiled DNA dose dependently. The RuvA-RuvB complex has an activity that renatures the cruciform structure in supercoiled DNA. From these experiments and previous work, we infer that the RuvA-RuvB complex may promote branch migration in recombination and may correct irregular structures in DNA, such as cruciforms and hairpins, to facilitate DNA repair using ATP as the energy source.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-2164626, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-2529252, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-2554134, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-2692243, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-2693946, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-2842314, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-2985470, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-3279394, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-3305513, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-3329215, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-344137, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-357368, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-374356, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-3891738, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-3960727, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-4590461, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-4907337, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-6295879, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-6371470, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-6374379, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-6577442, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-7021553, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-7045124, http://linkedlifedata.com/resource/pubmed/commentcorrection/1833759-7045590
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, 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, Superhelical, http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Holliday junction DNA helicase, E..., http://linkedlifedata.com/resource/pubmed/chemical/RuvB protein, Bacteria
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
88
pubmed:geneSymbol
ruvA, ruvB
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8445-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
SOS-inducible DNA repair proteins, RuvA and RuvB, of Escherichia coli: functional interactions between RuvA and RuvB for ATP hydrolysis and renaturation of the cruciform structure in supercoiled DNA.
pubmed:affiliation
Department of Experimental Chemotherapy, Osaka University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't