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Structure specific DNA recognition by the SLX1-SLX4 endonuclease complex.
Xu, Xiang; Wang, Mingzhu; Sun, Jixue; Yu, Zhenyu; Li, Guohong; Yang, Na; Xu, Rui-Ming.
Affiliation
  • Xu X; State Key Laboratory of Medicinal Chemical Biology, College of Pharmacy and Key Laboratory of Medical Data Analysis and Statistical Research of Tianjin, Nankai University, Tianjin 300353, China.
  • Wang M; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
  • Sun J; Institutes of Physical Science and Information Technology, Anhui University, Hefei 230601, Anhui, China.
  • Yu Z; State Key Laboratory of Medicinal Chemical Biology, College of Pharmacy and Key Laboratory of Medical Data Analysis and Statistical Research of Tianjin, Nankai University, Tianjin 300353, China.
  • Li G; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
  • Yang N; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
  • Xu RM; School of Life Science, University of Chinese Academy of Sciences, Beijing 100049, China.
Nucleic Acids Res ; 49(13): 7740-7752, 2021 07 21.
Article in En | MEDLINE | ID: mdl-34181713
The SLX1-SLX4 structure-specific endonuclease complex is involved in processing diverse DNA damage intermediates, including resolution of Holliday junctions, collapse of stalled replication forks and removal of DNA flaps. The nuclease subunit SLX1 is inactive on its own, but become activated upon binding to SLX4 via its conserved C-terminal domain (CCD). Yet, how the SLX1-SLX4 complex recognizes specific DNA structure and chooses cleavage sites remains unknown. Here we show, through a combination of structural, biochemical and computational analyses, that the SAP domain of SLX4 is critical for efficient and accurate processing of 5'-flap DNA. It binds the minor groove of DNA about one turn away from the flap junction, and the 5'-flap is implicated in binding the core domain of SLX1. This binding mode accounts for specific recognition of 5'-flap DNA and specification of cleavage site by the SLX1-SLX4 complex.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Saccharomyces cerevisiae Proteins / Endodeoxyribonucleases Language: En Journal: Nucleic Acids Res Year: 2021 Document type: Article Affiliation country: China Country of publication: United kingdom

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Saccharomyces cerevisiae Proteins / Endodeoxyribonucleases Language: En Journal: Nucleic Acids Res Year: 2021 Document type: Article Affiliation country: China Country of publication: United kingdom