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rdf:type |
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lifeskim:mentions |
umls-concept:C0002520,
umls-concept:C0012854,
umls-concept:C0026200,
umls-concept:C0028326,
umls-concept:C1135858,
umls-concept:C1145667,
umls-concept:C1415222,
umls-concept:C1514562,
umls-concept:C1552866,
umls-concept:C1706044,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2700399
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pubmed:issue |
1
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pubmed:dateCreated |
1998-12-17
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pubmed:abstractText |
GST-NS1 purified from Escherichia coli and insect cells binds double-strand DNA in an (ACCA)2-3-dependent fashion under similar ionic conditions, independent of the presence of anti-NS1 antisera or exogenously supplied ATP and interacts with single-strand DNA and RNA in a sequence-independent manner. An amino-terminal domain (amino acids 1-275) of NS1 [GST-NS1(1-275)], representing 41% of the full-length NS1 molecule, includes a domain that binds double-strand DNA in a sequence-specific manner at levels comparable to full-length GST-NS1, as well as single-strand DNA and RNA in a sequence-independent manner. The deletion of 15 additional amino-terminal amino acids yielded a molecule [GST-NS1(1-275)] that maintained (ACCA)2-3-specific double-strand DNA binding; however, this molecule was more sensitive to increasing ionic conditions than full-length GST-NS1 and GST-NS1(1-275) and could not be demonstrated to bind single-strand nucleic acids. A quantitative filter binding assay showed that E. coli- and baculovirus-expressed GST-NS1 and E. coli GST-NS1(1-275) specifically bound double-strand DNA with similar equilibrium kinetics [as measured by their apparent equilibrium DNA binding constants (KD)], whereas GST-NS1(16-275) bound 4- to 8-fold less well.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Single-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NS1 protein, minute virus of mice,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Nonstructural Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0042-6822
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 1998 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
251
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
123-31
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9813208-Adenosine Triphosphate,
pubmed-meshheading:9813208-Amino Acids,
pubmed-meshheading:9813208-Animals,
pubmed-meshheading:9813208-Baculoviridae,
pubmed-meshheading:9813208-Base Sequence,
pubmed-meshheading:9813208-Binding Sites,
pubmed-meshheading:9813208-DNA,
pubmed-meshheading:9813208-DNA, Single-Stranded,
pubmed-meshheading:9813208-DNA-Binding Proteins,
pubmed-meshheading:9813208-Escherichia coli,
pubmed-meshheading:9813208-Mice,
pubmed-meshheading:9813208-Minute virus of mice,
pubmed-meshheading:9813208-Osmolar Concentration,
pubmed-meshheading:9813208-Protein Conformation,
pubmed-meshheading:9813208-RNA,
pubmed-meshheading:9813208-Recombinant Fusion Proteins,
pubmed-meshheading:9813208-Sequence Deletion,
pubmed-meshheading:9813208-Thermodynamics,
pubmed-meshheading:9813208-Viral Nonstructural Proteins
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pubmed:year |
1998
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pubmed:articleTitle |
Amino acids 16-275 of minute virus of mice NS1 include a domain that specifically binds (ACCA)2-3-containing DNA.
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pubmed:affiliation |
School of Medicine, University of Missouri, Columbia, Missouri, 65212, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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