Structural basis for the recognition of sulfur in phosphorothioated DNA

Guang Liu, Wencheng Fu, Zhenyi Zhang, Yao He, Hao Yu, Yuli Wang, Xiaolei Wang, Yi-Lei Zhao, Zixin Deng, Geng Wu () and Xinyi He ()
Additional contact information
Guang Liu: Shanghai Jiao Tong University
Wencheng Fu: Shanghai Jiao Tong University
Zhenyi Zhang: Shanghai Jiao Tong University
Yao He: King Abdullah University of Science and Technology
Hao Yu: Shanghai Jiao Tong University
Yuli Wang: Shanghai Jiao Tong University
Xiaolei Wang: Shanghai Jiao Tong University
Yi-Lei Zhao: Shanghai Jiao Tong University
Zixin Deng: Shanghai Jiao Tong University
Geng Wu: Shanghai Jiao Tong University
Xinyi He: Shanghai Jiao Tong University

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract There have been very few reports on protein domains that specifically recognize sulfur. Here we present the crystal structure of the sulfur-binding domain (SBD) from the DNA phosphorothioation (PT)-dependent restriction endonuclease ScoMcrA. SBD contains a hydrophobic surface cavity that is formed by the aromatic ring of Y164, the pyrolidine ring of P165, and the non-polar side chains of four other residues that serve as lid, base, and wall of the cavity. The SBD and PT-DNA undergo conformational changes upon binding. The S187RGRR191 loop inserts into the DNA major groove to make contacts with the bases of the GPSGCC core sequence. Mutating key residues of SBD impairs PT-DNA association. More than 1000 sequenced microbial species from fourteen phyla contain SBD homologs. We show that three of these homologs bind PT-DNA in vitro and restrict PT-DNA gene transfer in vivo. These results show that SBD-like PT-DNA readers exist widely in prokaryotes.

Date: 2018
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-018-07093-1 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07093-1

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-018-07093-1

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().