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- Title
hMutSalpha forms an ATP-dependent complex with hMutLalpha and hMutLbeta on DNA.
- Authors
Plotz, Guido; Raedle, Jochen; Brieger, Angela; Trojan, Jörg; Zeuzem, Stefan
- Abstract
The DNA binding properties of hMutSalpha and hMutLalpha and complex formation of hMutSalpha with hMutLalpha and hMutLbeta were investigated using binding experiments on magnetic bead-coupled DNA substrates with nuclear extracts as well as purified proteins. hMutSalpha binding to homoduplex DNA was disrupted by lower NaCl concentrations than hMutSalpha binding to a mismatch. ATP markedly reduced the salt resistance of hMutSalpha binding but hMutSalpha still retained affinity for heteroduplexes. hMutSalpha formed a complex with hMutLalpha and hMutLbeta on DNA in the presence of ATP. This complex only formed on 81mer and not 32mer DNA substrates. Complex formation was enhanced by a mismatch in the DNA substrate, and hMutLalpha and hMutLbeta were shown to enter the complex at different ATP concentrations. Purified hMutLalpha showed an intrinsic affinity for DNA, with a preference for single-stranded over double-stranded DNA.
- Publication
Nucleic acids research, 2002, Vol 30, Issue 3, p711
- ISSN
1362-4962
- Publication type
Journal Article
- DOI
10.1093/nar/30.3.711