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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2002-12-24
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pubmed:abstractText |
The N-terminal domain of the Escherichia coli Ada protein (N-Ada) repairs methyl phosphotriesters in DNA through a zinc-mediated transfer to Cys38 of the protein. Methylation of Cys38 enhances the sequence-specific DNA affinity of N-Ada by approximately 1000-fold, thereby enabling the protein to activate the genes of a methylation-resistance regulon. It is of interest to understand the structural basis for metalloactivated methyl transfer and methylation-dependent enhancement of DNA binding activity. Although recent progress has been made on the structural front, efforts to develop a complete picture of N-Ada structure/function have been hampered by the inability to prepare homogeneous protein/DNA complexes representing different states of the unmethylated protein. Here, we describe the development of an approach to trap both sequence-specific and nonsequence-specific DNA recognition complexes of N-Ada through formation of an intermolecular disulfide crosslink between the protein and DNA.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1074-5521
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1297-303
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12498882-Bacterial Proteins,
pubmed-meshheading:12498882-Base Sequence,
pubmed-meshheading:12498882-Binding Sites,
pubmed-meshheading:12498882-Cross-Linking Reagents,
pubmed-meshheading:12498882-DNA,
pubmed-meshheading:12498882-DNA-Binding Proteins,
pubmed-meshheading:12498882-Disulfides,
pubmed-meshheading:12498882-Escherichia coli Proteins,
pubmed-meshheading:12498882-Methylation,
pubmed-meshheading:12498882-Molecular Probe Techniques,
pubmed-meshheading:12498882-Mutation,
pubmed-meshheading:12498882-O(6)-Methylguanine-DNA Methyltransferase,
pubmed-meshheading:12498882-Protein Binding,
pubmed-meshheading:12498882-Transcription Factors
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pubmed:year |
2002
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pubmed:articleTitle |
Trapping distinct structural states of a protein/DNA interaction through disulfide crosslinking.
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pubmed:affiliation |
Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138, 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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