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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Krasteva, Petya V. Harwood, Caroline S. Matsuyama, Bruno Y. Baraquet, Claudine Sondermann, Holger Navarro, Marcos V. A. S. |
| Description | Author Affiliation: Matsuyama BY ( Departamento de Física e Ciência Interdisciplinar, Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos 13563-120, SP, Brazil); Krasteva PV ( Department of Structural Biology and Chemistry, Unité G5 Biologie Structurale de la Sécrétion Bactérienne and UMR 3528, CNRS, Institut Pasteur, 75015 Paris, France); Baraquet C ( Department of Microbiology, University of Washington, Seattle, WA 98195.); Harwood CS ( Department of Microbiology, University of Washington, Seattle, WA 98195 csh5@uw.edu hs293@cornell.edu mvasnavarro@ifsc.usp.br.); Sondermann H ( Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853); Navarro MV ( Departamento de Física e Ciência Interdisciplinar, Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos 13563-120, SP, Brazil); |
| Abstract | Bacterial biofilm formation during chronic infections confers increased fitness, antibiotic tolerance, and cytotoxicity. In many pathogens, the transition from a planktonic lifestyle to collaborative, sessile biofilms represents a regulated process orchestrated by the intracellular second-messenger c-di-GMP. A main effector for c-di-GMP signaling in the opportunistic pathogen Pseudomonas aeruginosa is the transcription regulator FleQ. FleQ is a bacterial enhancer-binding protein (bEBP) with a central AAA+ ATPase σ(54)-interaction domain, flanked by a C-terminal helix-turn-helix DNA-binding motif and a divergent N-terminal receiver domain. Together with a second ATPase, FleN, FleQ regulates the expression of flagellar and exopolysaccharide biosynthesis genes in response to cellular c-di-GMP. Here we report structural and functional data that reveal an unexpected mode of c-di-GMP recognition that is associated with major conformational rearrangements in FleQ. Crystal structures of FleQ's AAA+ ATPase domain in its apo-state or bound to ADP or ATP-γ-S show conformations reminiscent of the activated ring-shaped assemblies of other bEBPs. As revealed by the structure of c-di-GMP-complexed FleQ, the second messenger interacts with the AAA+ ATPase domain at a site distinct from the ATP binding pocket. c-di-GMP interaction leads to active site obstruction, hexameric ring destabilization, and discrete quaternary structure transitions. Solution and cell-based studies confirm coupling of the ATPase active site and c-di-GMP binding, as well as the functional significance of crystallographic interprotomer interfaces. Taken together, our data offer unprecedented insight into conserved regulatory mechanisms of gene expression under direct c-di-GMP control via FleQ and FleQ-like bEBPs. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 2 |
| Volume Number | 113 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2016-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Bacterial Proteins Metabolism Biofilms Drug Effects Cyclic GMP Analogs & Derivatives Pseudomonas Aeruginosa Physiology Trans-Activators Amino Acid Motifs Amino Acid Sequence Chemistry Binding Sites Calorimetry Conserved Sequence Cross-Linking Reagents Crystallography, X-Ray Pharmacology DNA, Bacterial Gene Expression Regulation, Bacterial Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Mutant Proteins Promoter Regions, Genetic Genetics Protein Multimerization Protein Stability Protein Structure, Quaternary Protein Structure, Tertiary Sequence Alignment Temperature Transcription, Genetic Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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