Characterization of Multi-Functional Properties and ConformationalAnalysis of MutS2 from Thermotoga maritima MSB8

Collection with item attached
2012
Item details URL
http://open-repository.kisti.re.kr/cube/handle/open_repository/475911.do
DOI
10.1371/journal.pone.0034529
Title
Characterization of Multi-Functional Properties and ConformationalAnalysis of MutS2 from Thermotoga maritima MSB8
Description
This work was supported by the National Research Foundation of Korea[NRF-20110013431] and by KOSEF through the Center for Electro-PhotoBehaviors in Advanced Molecular Systems [20110007166]. The funders hadno role in study design, data collection and analysis, decision topublish, or preparation of the manuscript.
abstract
The MutS2 homologues have received attention because of their unusual activities that differ from those of MutS. In this work, we report on the functional characteristics and conformational diversities of Thermotoga maritima MutS2 (TmMutS2). Various biochemical features of the protein were demonstrated via diverse techniques such as scanning probe microscopy (SPM), ATPase assays, analytical ultracentrifugation, DNA binding assays, size chromatography, and limited proteolytic analysis. Dimeric TmMutS2 showed the temperature-dependent ATPase activity. The non-specific nicking endonuclease activities of TmMutS2 were inactivated in the presence of nonhydrolytic ATP (ADPnP) and enhanced by the addition of TmMutL. In addition, TmMutS2 suppressed the TmRecA-mediated DNA strand exchange reaction in a TmMutL-dependent manner. We also demonstrated that small-angle X-ray scattering (SAXS) analysis of dimeric TmMutS2 exhibited nucleotide- and DNA-dependent conformational transitions. Particularly, TmMutS2-ADPnP showed the most compressed form rather than apo-TmMutS2 and the TmMutS2-ADP complex, in accordance with the results of biochemical assays. In the case of the DNA-binding complexes, the stretched conformation appeared in the TmMutS2-four-way junction (FWJ)-DNA complex. Convergences of biochemical-and SAXS analysis provided abundant information for TmMutS2 and clarified ambiguous experimental results.
provenance
Made available in Cube on 2018-09-28T11:25:28Z (GMT). No. of bitstreams: 0
language
English
author
Jeong, Euiyoung
Jo, Hunho
Kim, Tae Gyun
Ban, Changill
accessioned
2018-09-28T11:25:28Z
available
2018-09-28T11:25:28Z
issued
2012
citation
PLOS ONE(7): 4
issn
1932-6203
uri
http://open-repository.kisti.re.kr/cube/handle/open_repository/475911.do
Funder
교육과학기술부
Funding Program
선도연구센터지원
Project ID
1345175456
Jurisdiction
Rep.of Korea
Project Name
Development of the early diagnostic and therapeutic methods for human disease using oligo-nucleotide and peptides
rights
openAccess
type
article


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