作者: Silvia L. Porello , Michelle J. Cannon , Sheila S. David
DOI: 10.1021/BI972433T
关键词: DNA replication 、 Ferrous 、 Biochemistry 、 Enzyme 、 DNA 、 DNA glycosylase 、 DNA repair 、 Nucleic acid 、 In vitro 、 Chemistry
摘要: The Escherichia coli DNA repair enzyme MutY plays an important role in the recognition and of 7,8-dihydro-8-oxo-2‘-deoxyguanosine: 2‘-deoxyadenosine (OG:A) mismatches [Michaels et al. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 7022−7025]. prevents mutations due to misincorporation A opposite OG during replication by removing adenine base. This has significant sequence homology with [4Fe-4S]2+ cluster-containing enzyme, endonuclease III (1990) Nucleic Acids Res. 18, 3841−3845]. In present study, we have investigated importance cluster assembly folding MutY. was denatured then refolded presence or absence ferrous sulfide ions. Denatured can refold ions provide active enzyme. suggests self-assemble that this process is facile vitro. Interestingly, CD spectra Tm measurements without sulfi...