期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 114, 期 24, 页码 E4822-E4831出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1702435114
关键词
c-di-GMP; transcription factor; PilZ; extracellular polysaccharide; Sinorhizobium meliloti
资金
- Deutsche Forschungsgemeinschaft through Collaborative Research Centre [SFB 987]
- Large Research Instrumentation Grants [INST 160/621-1 FUGG, INST 160/536-1 FUGG]
- LOEWE Excellence Initiative of the State of Hesse, Germany
- Max Planck Society
Cyclic dimeric GMP (c-di-GMP) has emerged as a key regulatory player in the transition between planktonic and sedentary biofilm-associated bacterial lifestyles. It controls a multitude of processes including production of extracellular polysaccharides (EPSs). The PilZ domain, consisting of an N-terminal RxxxR motif and a beta-barrel domain, represents a prototype c-di-GMP receptor. We identified a class of c-di-GMP-responsive proteins, represented by the AraC-like transcription factor CuxR in plant symbiotic alpha-proteobacteria. In Sinorhizobium meliloti, CuxR stimulates transcription of an EPS biosynthesis gene cluster at elevated c-di-GMP levels. CuxR consists of a Cupin domain, a helical hairpin, and bipartite helix-turn-helix motif. Although unrelated in sequence, the mode of c-di-GMP binding to CuxR is highly reminiscent to that of PilZ domains. c-di-GMP interacts with a conserved N-terminal RxxxR motif and the Cupin domain, thereby promoting CuxR dimerization and DNA binding. We unravel structure and mechanism of a previously unrecognized c-di-GMP-responsive transcription factor and provide insights into the molecular evolution of c-di-GMP binding to proteins.
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