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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
1985-11-29
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pubmed:abstractText |
We demonstrate by agarose gel electrophoresis and DNase I footprinting that Xenopus transcription factor A promotes DNA reassociation. This ability of factor A is dependent upon the domain-like structure of the protein. Digestion of factor A by papain results in a protein fragment which promotes DNA reassociation whereas a smaller fragment obtained by trypsin digestion does not. Although factor A requires zinc for specific binding to the 5 S RNA gene, the metal is not required for single-stranded DNA binding or promotion of DNA reassociation by this protein. The factor A-dependent renaturation of the 5 S RNA gene from its individual 32P end-labeled strands results in the proper gene conformation as evidenced by the restoration of the DNase I footprint characteristic of the intragenic control region. Alterations in DNase I cleavage patterns induced by factor A on the individual 5 S DNA strands are distinct from those induced by the protein on the duplex 5 S RNA gene. The ability of factor A to promote DNA reassociation further defines the possible roles of this protein in the formation of active transcription complexes and their maintenance during repeated rounds of transcription.
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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/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Single-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease I,
http://linkedlifedata.com/resource/pubmed/chemical/Papain,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/TFAM protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/XL-MTTFA protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
260
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13316-20
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2414278-Animals,
pubmed-meshheading:2414278-DNA,
pubmed-meshheading:2414278-DNA, Single-Stranded,
pubmed-meshheading:2414278-Deoxyribonuclease I,
pubmed-meshheading:2414278-Nucleic Acid Denaturation,
pubmed-meshheading:2414278-Nucleic Acid Renaturation,
pubmed-meshheading:2414278-Papain,
pubmed-meshheading:2414278-Peptide Fragments,
pubmed-meshheading:2414278-RNA,
pubmed-meshheading:2414278-Structure-Activity Relationship,
pubmed-meshheading:2414278-Trans-Activators,
pubmed-meshheading:2414278-Transcription, Genetic,
pubmed-meshheading:2414278-Transcription Factors,
pubmed-meshheading:2414278-Trypsin,
pubmed-meshheading:2414278-Xenopus Proteins,
pubmed-meshheading:2414278-Xenopus laevis,
pubmed-meshheading:2414278-Zinc
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pubmed:year |
1985
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pubmed:articleTitle |
Xenopus transcription factor A promotes DNA reassociation.
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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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