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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1995-8-10
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pubmed:abstractText |
High-mobility-group protein 1 (HMG1) is an abundant, non-sequence-specific, chromosomal protein with two homologous, HMG-box, DNA-binding domains, A and B, and an acidic tail. The HMG-box motif also occurs, as a single copy, in some sequence-specific transcription factors, e.g. the sex-determining factor, SRY. We have investigated whether or not there are differences in the DNA-binding properties of the isolated A and B HMG-box domains of HMG1 and SRY and whether, in the case of A and B, there might also be differences due to different sequence contexts within the native protein. The basic regions that flank the HMG1 B box, giving B', enhance its DNA-binding, supercoiling and DNA-bending activities, and promote the self-association of the DNA-bound B-box. All the HMG-box domains bind with structure specificity to four-way junctions, but the structure selectivity is significantly greater for A and the SRY box than for the HMG1 B or B' domains, as judged by competition with excess plasmid DNA. The domains self-associate to different extents on supercoiled DNA and this may explain differences in the ability to discriminate between four-way junctions and supercoiled DNA. The HMG1 A, B and B' domains constrain negative superhelical turns in DNA, but the SRY HMG box does not. Only the full B domain (B') bends DNA in a ligase-mediated circularisation assay; the minimal B box, the A domain and the SRY box do not. Thus, despite a common global fold, the HMG box appears to have been adapted to various functions in different protein contexts.
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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/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Superhelical,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/High Mobility Group Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sex-Determining Region Y Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
230
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
943-50
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:7601157-Amino Acid Sequence,
pubmed-meshheading:7601157-DNA,
pubmed-meshheading:7601157-DNA, Superhelical,
pubmed-meshheading:7601157-DNA-Binding Proteins,
pubmed-meshheading:7601157-High Mobility Group Proteins,
pubmed-meshheading:7601157-Molecular Sequence Data,
pubmed-meshheading:7601157-Nuclear Proteins,
pubmed-meshheading:7601157-Sex-Determining Region Y Protein,
pubmed-meshheading:7601157-Transcription Factors
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pubmed:year |
1995
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pubmed:articleTitle |
Differences in the DNA-binding properties of the HMG-box domains of HMG1 and the sex-determining factor SRY.
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pubmed:affiliation |
Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, England.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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