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Nucleic Acids Research, 2002, Vol. 30, No. 3 711-718
© 2002 Oxford University Press

hMutS{alpha} forms an ATP-dependent complex with hMutL{alpha} and hMutLß on DNA

Guido Plotz, Jochen Raedle, Angela Brieger, Jörg Trojan and Stefan Zeuzem*

Second Department of Medicine, Johann Wolfgang Goethe-University, Theodor Stern-Kai 7, D-60590 Frankfurt am Main, Germany

The DNA binding properties of hMutS{alpha} and hMutL{alpha} and complex formation of hMutS{alpha} with hMutL{alpha} and hMutLß were investigated using binding experiments on magnetic bead-coupled DNA substrates with nuclear extracts as well as purified proteins. hMutS{alpha} binding to homoduplex DNA was disrupted by lower NaCl concentrations than hMutS{alpha} binding to a mismatch. ATP markedly reduced the salt resistance of hMutS{alpha} binding but hMutS{alpha} still retained affinity for heteroduplexes. hMutS{alpha} formed a complex with hMutL{alpha} and hMutLß 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 hMutL{alpha} and hMutLß were shown to enter the complex at different ATP concentrations. Purified hMutL{alpha} showed an intrinsic affinity for DNA, with a preference for single-stranded over double-stranded DNA.

* To whom correspondence should be addressed. Tel: +49 69 6301 5297; Fax: +49 69 6301 4807; Email: zeuzem{at}em.uni-frankfurt.de


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