DNA glycosylase
From Proteopedia
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'''DNA glycosylase''' (DG) are enzymes which remove damaged DNA bases by flipping them out of the double helix followed by their cleavage. Monofunctional DG have only glycosylase activity; bifunctional DG also act as lysates; ADG, UDG, TDG remove adenine, uracil, thymine from DNA.<ref>PMID:15102448</ref><br /> | '''DNA glycosylase''' (DG) are enzymes which remove damaged DNA bases by flipping them out of the double helix followed by their cleavage. Monofunctional DG have only glycosylase activity; bifunctional DG also act as lysates; ADG, UDG, TDG remove adenine, uracil, thymine from DNA.<ref>PMID:15102448</ref><br /> | ||
* '''Adenine DNA glycosylase''' is also called '''MutY'''. MutY has a role in prevention of DNA mutations resulting from oxidative damage forming the mutated base oxoG. DNA polymerase misreads oxoG and pairs it with adenine instead of cytosine. MutY removes adenine from the mismatched oxoG:A pair. MutY contains a 4Fe4S cluster.<br /> | * '''Adenine DNA glycosylase''' is also called '''MutY'''. MutY has a role in prevention of DNA mutations resulting from oxidative damage forming the mutated base oxoG. DNA polymerase misreads oxoG and pairs it with adenine instead of cytosine. MutY removes adenine from the mismatched oxoG:A pair. MutY contains a 4Fe4S cluster.<br /> | ||
| - | * '''Uracil DNA glycosylase''' (UDG) eliminates uracil from DNA and thus preventing mutagenesis. UDG initiates the base excision repair pathway. UDG excises uracil in both AU and GU pairs. UDG can repair 10,000 damaged bases in the human cell per day<ref>PMID:9882380</ref>. | + | * '''Uracil DNA glycosylase''' (UDG) eliminates uracil from DNA and thus preventing mutagenesis. UDG initiates the base excision repair pathway. UDG excises uracil in both AU and GU pairs. UDG can repair 10,000 damaged bases in the human cell per day<ref>PMID:9882380</ref>. See also [[DNA Repair]]. |
* '''Thymine DNA glycosylase''' removes thymine moieties from mismatched G/T, C/T and T/T.<br /> | * '''Thymine DNA glycosylase''' removes thymine moieties from mismatched G/T, C/T and T/T.<br /> | ||
* '''Smug1''' is a single-strand selective monofunctional UDG. <br /> | * '''Smug1''' is a single-strand selective monofunctional UDG. <br /> | ||
Current revision
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References
- ↑ Fromme JC, Banerjee A, Verdine GL. DNA glycosylase recognition and catalysis. Curr Opin Struct Biol. 2004 Feb;14(1):43-9. PMID:15102448 doi:http://dx.doi.org/10.1016/j.sbi.2004.01.003
- ↑ Willetts KE, Rey F, Agostini I, Navarro JM, Baudat Y, Vigne R, Sire J. DNA repair enzyme uracil DNA glycosylase is specifically incorporated into human immunodeficiency virus type 1 viral particles through a Vpr-independent mechanism. J Virol. 1999 Feb;73(2):1682-8. PMID:9882380
- ↑ Fromme JC, Banerjee A, Huang SJ, Verdine GL. Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase. Nature. 2004 Feb 12;427(6975):652-6. PMID:14961129 doi:10.1038/nature02306
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