期刊
MOLECULAR MICROBIOLOGY
卷 93, 期 3, 页码 439-452出版社
WILEY
DOI: 10.1111/mmi.12672
关键词
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资金
- United States National Science Foundation [MCB1052575]
- NIH Intramural Research Program at the National Library of Medicine
- Swedish Research Council Natural Sciences [621-2010-5755]
- Petrus and Augusta Hedlund Foundation
- Carl Tryggers Foundation [CTS 10: 324]
- International Research Training Group 1273 - German Research Foundation (DFG)
- NIH Intramural Research Program at the National Library of Medicine [ZIA LM000073-14]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1052575] Funding Source: National Science Foundation
In contrast to numerous enzymes involved in c-di-GMP synthesis and degradation in enterobacteria, only a handful of c-di-GMP receptors/effectors have been identified. In search of new c-di-GMP receptors, we screened the Escherichia coli ASKA overexpression gene library using the Differential Radial Capillary Action of Ligand Assay (DRaCALA) with fluorescently and radioisotope-labelled c-di-GMP. We uncovered three new candidate c-di-GMP receptors in E. coli and characterized one of them, BcsE. The bcsE gene is encoded in cellulose synthase operons in representatives of Gammaproteobacteria and Betaproteobacteria. The purified BcsE proteins from E. coli, Salmonella enterica and Klebsiella pneumoniae bind c-di-GMP via the domain of unknown function, DUF2819, which is hereby designated GIL, GGDEF I-site like domain. The RxGD motif of the GIL domain is required for c-di-GMP binding, similar to the c-di-GMP-binding I-site of the diguanylate cyclase GGDEF domain. Thus, GIL is the second protein domain, after PilZ, dedicated to c-di-GMP-binding. We show that in S. enterica, BcsE is not essential for cellulose synthesis but is required for maximal cellulose production, and that c-di-GMP binding is critical for BcsE function. It appears that cellulose production in enterobacteria is controlled by a two-tiered c-di-GMP-dependent system involving BcsE and the PilZ domain containing glycosyltransferase BcsA.
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