Abstract:
:Recognizing the methylation status of specific DNA sequences is central to the function of many systems in eukaryotes and prokaryotes. Restriction-modification systems have to distinguish between 'self' and 'non-self' DNA and depend on the inability of restriction endonucleases to cleave their DNA substrates when the DNA is appropriately methylated. These endonucleases thus provide a model system for studying the recognition of DNA methylation by proteins. We have characterized the interaction of R.PVU:II with DNA containing the physiologically relevant N4-methylcytosine modification. R.PVU:II binds (N4m)C-modified DNA and cleaves it very slowly. Methylated strands in hemimethylated duplexes were cleaved at a higher rate than in fully methylated duplexes, in parallel with a higher binding affinity for hemimethylated DNA. The co-crystal structures of R.PVU:II-DNA, together with a mutagenesis study, have implicated specific amino acids in recognition of the methylatable base; one of these is His84. We report that replacing His84 with Ala reduced the rate of cleavage of unmodified DNA but, in contrast, slightly increased the cleavage of (N4m)C-modified DNA.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Rice MR,Blumenthal RMdoi
10.1093/nar/28.16.3143keywords:
subject
Has Abstractpub_date
2000-08-15 00:00:00pages
3143-50issue
16eissn
0305-1048issn
1362-4962journal_volume
28pub_type
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更新日期:1977-01-01 00:00:00
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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更新日期:2014-05-01 00:00:00
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journal_title:Nucleic acids research
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更新日期:2005-08-09 00:00:00
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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