rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1993-5-14
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pubmed:abstractText |
The DNA binding domain of the interferon regulatory factor-2 protein (IRF-2) has been produced and characterized. alpha-chymotrypsin digestion of the purified IRF-2 protein bound to a synthetic binding site yields a peptide fragment of 14 K in molecular weight. N-terminal analysis of this peptide fragment showed that its sequence is the same as that of the intact IRF-2. A peptide fragment of approximately 14 K, IRF-2(113), which corresponds to the N-terminal 113 amino acids of the intact IRF-2 protein, has been expressed in a functional form in Escherichia coli. The first methionine was processed during the expression and the purified IRF-2(113) thus contains 112 amino acids. DNase I footprinting and gel retardation assaying showed that IRF-2(113) binds to a synthetic DNA having the consensus binding site and to the upstream regulatory sequence of the IFN-beta gene as intact IRF-2 does. These results showed that this peptide fragment, IRF-2(113), may be a good material for investigation of the DNA binding domain of IRF-2 and of the DNA-protein interaction.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Feb
|
pubmed:issn |
0269-2139
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
6
|
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
195-200
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8475044-Amino Acid Sequence,
pubmed-meshheading:8475044-Animals,
pubmed-meshheading:8475044-Base Sequence,
pubmed-meshheading:8475044-Binding Sites,
pubmed-meshheading:8475044-Circular Dichroism,
pubmed-meshheading:8475044-DNA,
pubmed-meshheading:8475044-DNA-Binding Proteins,
pubmed-meshheading:8475044-Escherichia coli,
pubmed-meshheading:8475044-Interferon Regulatory Factor-2,
pubmed-meshheading:8475044-Mice,
pubmed-meshheading:8475044-Molecular Sequence Data,
pubmed-meshheading:8475044-Peptide Fragments,
pubmed-meshheading:8475044-Protein Binding,
pubmed-meshheading:8475044-Protein Structure, Secondary,
pubmed-meshheading:8475044-Protein Structure, Tertiary,
pubmed-meshheading:8475044-Recombinant Fusion Proteins,
pubmed-meshheading:8475044-Repressor Proteins,
pubmed-meshheading:8475044-Transcription Factors
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pubmed:year |
1993
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pubmed:articleTitle |
Characterization of the DNA binding domain of the mouse IRF-2 protein.
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pubmed:affiliation |
Institute for Protein Research, Osaka University, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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