stimulation of dna glycosylase activities by xpc protein complex roles of protein-protein interactions刺激的dna糖基化酶活动xpc蛋白质蛋白质相互作用的复杂角色.pdf

SAGE-Hindawi Access to Research Journal of Nucleic Acids Volume 2010, Article ID 805698, 12 pages doi:10.4061/2010/805698 Research Article Stimulation of DNA Glycosylase Activities by XPC Protein Complex: Roles of Protein-Protein Interactions Yuichiro Shimizu,1, 2 Yasuhiro Uchimura,3 Naoshi Dohmae,4 Hisato Saitoh,3 Fumio Hanaoka,1, 2 and Kaoru Sugasawa1, 5 1 Cellular Physiology Laboratory, RIKEN Discovery Research Institute, Wako, Saitama 351-0198, Japan 2 Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan 3 Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University, Kumamoto 860-8555, Japan 4 Biomolecular Characterization Team, RIKEN Discovery Research Institute, Wako, Saitama 351-0198, Japan 5 Biosignal Research Center, Organization of Advanced Science and Technology, Kobe University, Kobe, Hyogo 657-8501, Japan Correspondence should be addressed to Kaoru Sugasawa, ksugasawa@garnet.kobe-u.ac.jp Received 30 April 2010; Accepted 9 June 2010 Academic Editor: Ashis Basu Copyright © 2010 Yuichiro Shimizu et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. We showed that XPC complex, which is a DNA damage detector for nucleotide excision repair, stimulates activity of thymine DNA glycosylase (TDG) that initiates base excision repair. XPC appeared to facilitate the enzymatic turnover of TDG by promoting displacement from its own product abasic site, although the precise mechanism underlying this stimulation has not been clarified. Here we show that XPC has only marginal effects on the activity of E. coli TDG hom