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- W2558951504 abstract "The (cytosine-5) DNA methyltransferase M.Hhal causesits target cytosine basetobeflipped completelyoutoftheDNA helix uponbinding. We have investigated theeffects ofreplacing thetarget cytosine byother, mismatched bases, including adenine, guanine, thymine anduracil. We findthatM.Hhal binds moretightly tosuchmismatched substrates andcan eventransfer a methyl grouptouracil ifa G:U mismatch ispresent. Other mismatched substrates in whichtheorphan guanine ischanged exhibit similar behavior. Overall, theaffinity ofDNAbinding correlates inversely withthestability ofthetarget basepair, while thenature ofthetarget baseappears irrelevant forcomplex formation. Thepresence ofa cofactor analog, S-adenosyl-L-homocysteine, greatly enhances theselectivity ofthemethyltransferase forcytosine at thetarget site. Wepropose that theDNAmethyltransferases haveevolved frommismatch binding proteins andthatbaseflipping was,andstill is, akeyelement inmanyDNA-enzyme interactions." @default.
- W2558951504 created "2016-12-08" @default.
- W2558951504 creator A5019769228 @default.
- W2558951504 date "1995-01-01" @default.
- W2558951504 modified "2023-09-23" @default.
- W2558951504 title "M.HhaI bindstightly tosubstrates containing mismatches atthetarget base" @default.
- W2558951504 hasPublicationYear "1995" @default.
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