Nucleic Acids Research, Vol 26, Issue 18 4153-4159, Copyright © 1998 by Oxford University Press
H Tachiki, R Kato, R Masui, K Hasegawa, H Itakura, K Fukuyama and S Kuramitsu
MutS protein binds to DNA and specifically recognizes mismatched or small
looped out heteroduplex DNA. In order to elucidate its structure- function
relationships, the domain structure of Thermus thermophilus MutS protein
was studied by performing denaturation experiments and limited proteolysis.
The former suggested that T. thermophilus MutS consists of at least three
domains with estimated stabilities of 12.3, 22.9 and 30.7 kcal/mol and the
latter revealed that it consists of four domains: A1 (N-terminus to residue
130), A2 (131-274), B (275-570) and C (571 to C-terminus). A gel
retardation assay indicated that T.thermophilus MutS interacts
non-specifically with double-stranded (ds), but not single-stranded DNA.
Among the proteolytic fragments, the B domain bound to dsDNA. On the basis
of these results we have proposed the domain organization of T.
thermophilus MutS and putative roles of these domains.
ARTICLES
Domain organization and functional analysis of Thermus thermophilus MutS protein [published erratum appears in Nucleic Acids Res 1998 Oct 15;26(20):following 4789]
Department of Biology, Graduate School of Science, Osaka University, 1- 1 Machikaneyama-cho, Toyonaka, Osaka 560-0043, Japan.
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