Skip Navigation


Journal of Biochemistry Advance Access originally published online on November 23, 2008
Journal of Biochemistry 2009 145(2):199-206; doi:10.1093/jb/mvn157
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Data
Right arrow All Versions of this Article:
145/2/199    most recent
mvn157v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Kim, T. G.
Right arrow Articles by Ban, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kim, T. G.
Right arrow Articles by Ban, C.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 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; and 2Department of Life Science, Pohang University of Science and Technology, Pohang, Gyungbuk 790-784, Korea

*To whom correspondence should be addressed: Tel: +82-54-279-2127, Fax: +82-54-279-3399, E-mail: 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 Escherichia 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 3D view of the previously unresolved full-length MutL molecule.

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

Abbreviations: MMR, Methyl-directed mismatch repair; TmL, Thermotoga maritima MSB8 MutL; SAXS, Small-angle X-ray scattering; DLS, Dynamic light scattering


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.