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The c-di-GMP recognition mechanism of the PilZ domain of bacterial cellulose synthase subunit A

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Title: The c-di-GMP recognition mechanism of the PilZ domain of bacterial cellulose synthase subunit A
Authors: Fujiwara, Takaaki Browse this author
Komoda, Keisuke Browse this author
Sakurai, Naofumi Browse this author
Tajima, Kenji Browse this author
Tanaka, Isao Browse this author
Yao, Min Browse this author →KAKEN DB
Keywords: X-ray crystallography
PilZ domain
Bacterial cellulose synthase
Binding stoichiometry
Isothermal titration calorimetry
Issue Date: 22-Feb-2013
Publisher: Elsevier
Journal Title: Biochemical and Biophysical Research Communications
Volume: 431
Issue: 4
Start Page: 802
End Page: 807
Publisher DOI: 10.1016/j.bbrc.2012.12.103
PMID: 23291177
Abstract: In some Proteobacteria and Firmicutes such as Pseudomonas aeruginosa, Vibrio cholerae, Xanthomonas campestris, and Clostridium difficile, cyclic dimeric guanosine monophosphate (c-di-GMP) is known to regulate cellular processes, including motility, biofilm formation, and virulence, as a second messenger. Cellulose production in Acetobacter xylinum, a model organism of cellulose biosynthesis, also depends on by cellular c-di-GMP level. In cellulose-synthesizing bacteria, a terminal complex localized in the cell membrane synthesizes cellulose and regulates the production of cellulose sensed by c-di-GMP. Although previous studies indicated that the PilZ domain conserved in cellulose synthase subunit A (CeSA) was part of a receptor for c-di-GMP, the recognition mechanism by PilZ domain of CeSA remains unclear. In the present study, we studied the interaction between c-di-GMP and the PilZ domain of CeSA from a structural viewpoint. First, we solved the crystal structure of the PilZ domain of CeSA from A. xylinum (AxCeSA-PilZ) at 2.1 angstrom resolution. Then, comparison of the sequence and structure of AxCeSA-PilZ to those of known structures of PilZ, such as VCA0042, PP4397, and PA4608, indicated the involvement of Lys573 and Arg643 of AxCeSA-PilZ in the recognition of c-di-GMP besides the RxxxR motif. Finally, the binding characteristics of c-di-GMP to AxCeSA-PilZ and mutants were determined with isothermal titration calorimetry, indicating that the residues corresponding to Lys573 and Arg643 in AxCeSA-PilZ generally contribute to the binding of c-di-GMP to PilZ. (C) 2013 Elsevier Inc. All rights reserved.
Type: article (author version)
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 藤原 孝彰

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