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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Life Science / Faculty of Advanced Life Science >
Peer-reviewed Journal Articles, etc >
The c-di-GMP recognition mechanism of the PilZ domain of bacterial cellulose synthase subunit A
| 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 | | c-di-GMP | | 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) |
| URI: | http://hdl.handle.net/2115/52657 |
| 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)
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Submitter: 藤原 孝彰
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