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Journal of Biochemistry Advance Access published online on November 23, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn157
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© The authors 2008. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Structural insights of the nucleotide dependent conformational changes of Thermotoga maritima MutL using small-angle X-ray scattering analysis

Tae Gyun Kim1, Hyung Jin Cha2, Hyung Ju Lee1, Seong-Dal Heo1, Kwan Yong Choi2, Ja kang Ku1 and Changill Ban1,*

1Department of Chemistry, 2Department of Life Science, Pohang University of Science and Technology, Pohang, Gyungbuk, 790-784, Korea

*To whom correspondence should be addressed: Prof. Changill Ban. Tel: +82-54-279-2127, Fax: +82-54-279-3399, Email: ciban{at}postech.ac.kr

Received October 20, 2008; Accepted November 14, 2008


  Abstract

MutL is required to assist the mismatch repair protein MutS during initiation of the methyl-directed mismatch repair (MMR) response in various organisms ranging from prokaryotes to eukaryotes. Despite this necessity, the inherent propensity of MutL to aggregate has led to significant difficulties in determining its biological relationship with other MMR-related proteins. Here, we perform analysis on the thermostable MutL protein found in Thermotoga maritima MSB8 (TmL). Size exclusion chromatographic analysis indicates the lack of aggregated forms with the exception of a dimeric TmL. Small-angle X-ray scattering (SAXS) analysis reveals that the solution structures of the full-length TmL and its corresponding complexes with nucleotides and ssDNA undergo conformational changes. The elucidated TmL SAXS model is superimposed to the crystal structure of the C-terminal domain of E. coli MutL. In addition, the N-terminal SAXS model of TmL exists as monomeric form, indicating that TmL has a structurally flexible N-terminal domain. TmL SAXS analysis can suggest a considerable possibility on a new three-dimensional view of the previously unresolved full-length MutL molecule.

Key Words: Methyl-directed mismatch repair, Thermotoga maritima MSB8 MutL, Small-angle X-ray scattering, conformational change, E. coli MutL


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