A Substrate Recognition Role for the [4Fe-4S]2+ Cluster of the DNA Repair Glycosylase MutY†

作者: Silvia L. Porello , Michelle J. Cannon , Sheila S. David

DOI: 10.1021/BI972433T

关键词: DNA replicationFerrousBiochemistryEnzymeDNADNA glycosylaseDNA repairNucleic acidIn vitroChemistry

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...

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