Processing of mispaired and unpaired bases in heteroduplex DNA in E. coli()

Radman, Miroslav; Dohet, Christiane; Jones, Madeleine; Doutriaux, Marie-Pascale; Laengle-Rouault, F.; Maenhaut-Michel, G.; Wagner, Robert E.

doi:10.1016/s0300-9084(85)80162-0

Cited by 6 publications

(1 citation statement)

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“…Repair is initiated by binding of MutS and MutL to the mismatch, followed by a MutH-mediated incision of the nonmethylated DNA strand at hemimethylated GATC sites. The nicked strand is then degraded past the site of mismatch, and DNA polymerase fills in the resulting gap (28,33,37). The very short patch MMR system of E. coli recognizes G/T mismatches at sites where cytosine is methylated by the Dcm methylase and restores them to G/C pairs (25,26,49).…”

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confidence: 99%

A Uve1p-Mediated Mismatch Repair Pathway in Schizosaccharomyces pombe

Kaur¹,

Fraser²,

Freyer

et al. 1999

Molecular and Cellular Biology

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UV damage endonuclease (Uve1p) from Schizosaccharomyces pombe was initially described as a DNA repair enzyme specific for the repair of UV light-induced photoproducts and proposed as the initial step in an alternative excision repair pathway. Here we present biochemical and genetic evidence demonstrating that Uve1p is also a mismatch repair endonuclease which recognizes and cleaves DNA 5 to the mispaired base in a strand-specific manner. The biochemical properties of the Uve1p-mediated mismatch endonuclease activity are similar to those of the Uve1p-mediated UV photoproduct endonuclease. Mutants lacking Uve1p display a spontaneous mutator phenotype, further confirming the notion that Uve1p plays a role in mismatch repair. These results suggest that Uve1p has a surprisingly broad substrate specificity and may function as a general type of DNA repair protein with the capacity to initiate mismatch repair in certain organisms.

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confidence: 99%