MUTYH DNA glycosylase: the rationale for removing undamaged bases from the DNA.

摘要: Maintenance of genetic stability is crucial for all organisms in order to avoid the onset deleterious diseases such as cancer. One many proveniences DNA base damage mammalian cells oxidative stress, arising from a variety endogenous and exogenous sources, generating highly mutagenic lesions. best characterized lesion 7,8-dihydro-8-oxoguanine (8-oxo-G), which can give rise substitution mutations (also known point mutations). This mutagenicity due miscoding potential 8-oxo-G that instructs most polymerases (pols) preferentially insert an Adenine (A) opposite instead appropriate Cytosine (C). If left unrepaired, A:8-oxo-G mispairs CG->AT transversion mutations. are proficiently recognized by MutY glycosylase homologue (MUTYH). MUTYH remove mispaired A A:8-oxo-G, giving way canonical excision repair (BER) ultimately restores undamaged Guanine (G). The importance this MUTYH-initiated pathway illustrated fact biallelic gene associated with hereditary colorectal cancer syndrome termed MUTYH-associated polyposis (MAP). In review, we will focus on MUTYH, its discovery recent data regarding cellular roles interaction partners. We discuss involvement protein BER acting together pol , faithfully incorporate C thus bypass correct manner. also outline current knowledge about regulation itself posttranslational modifications (PTM). Finally, achieve clearer overview literature, briefly touch rather confusing nomenclature. short, unique catalyzes DNA.