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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3-4
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pubmed:dateCreated |
2000-11-13
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pubmed:abstractText |
Deamination of cytosine to uracil is one of the major pro-mutagenic events in DNA, causing G:C-->A:T transition mutations if not repaired before replication. Repair of uracil-DNA is achieved in a base-excision pathway initiated by a uracil-DNA glycosylase (UDG) enzyme of which four families have so far been identified. Family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by 'base-sampling' probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. This allows a broader specificity so that some Family-2 enzymes can excise uracil and 3, N(4)-ethenocytosine from mismatches with guanine. Although structures are not yet available for Family-3 (SMUG) and Family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family.
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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/3,N(4)-ethenocytosine,
http://linkedlifedata.com/resource/pubmed/chemical/Archaeal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytosine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Glycosylases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Glycosyl Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Thymine DNA Glycosylase,
http://linkedlifedata.com/resource/pubmed/chemical/Uracil,
http://linkedlifedata.com/resource/pubmed/chemical/Uracil-DNA Glycosidase,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/mismatch-specific thymine...
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0027-5107
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
460
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
165-81
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10946227-Amino Acid Sequence,
pubmed-meshheading:10946227-Archaeal Proteins,
pubmed-meshheading:10946227-Bacterial Proteins,
pubmed-meshheading:10946227-Base Pairing,
pubmed-meshheading:10946227-Cytosine,
pubmed-meshheading:10946227-DNA,
pubmed-meshheading:10946227-DNA Damage,
pubmed-meshheading:10946227-DNA Glycosylases,
pubmed-meshheading:10946227-DNA Repair,
pubmed-meshheading:10946227-Deamination,
pubmed-meshheading:10946227-Escherichia coli,
pubmed-meshheading:10946227-Escherichia coli Proteins,
pubmed-meshheading:10946227-Herpesvirus 1, Human,
pubmed-meshheading:10946227-Models, Molecular,
pubmed-meshheading:10946227-Molecular Sequence Data,
pubmed-meshheading:10946227-Multigene Family,
pubmed-meshheading:10946227-N-Glycosyl Hydrolases,
pubmed-meshheading:10946227-Point Mutation,
pubmed-meshheading:10946227-Protein Binding,
pubmed-meshheading:10946227-Protein Conformation,
pubmed-meshheading:10946227-Sequence Alignment,
pubmed-meshheading:10946227-Sequence Homology, Amino Acid,
pubmed-meshheading:10946227-Structure-Activity Relationship,
pubmed-meshheading:10946227-Substrate Specificity,
pubmed-meshheading:10946227-Thermotoga maritima,
pubmed-meshheading:10946227-Thymine DNA Glycosylase,
pubmed-meshheading:10946227-Uracil,
pubmed-meshheading:10946227-Uracil-DNA Glycosidase,
pubmed-meshheading:10946227-Viral Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
Structure and function in the uracil-DNA glycosylase superfamily.
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pubmed:affiliation |
Section of Structural Biology and CRC DNA Repair Enzyme Group, Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, SW3 6JB, London, UK. laurence@icr.ac.uk
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pubmed:publicationType |
Journal Article,
Comparative Study,
Review,
Research Support, Non-U.S. Gov't
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