The Hybrid Sensor Kinase RscS Integrates Positive and Negative Signals To Modulate Biofilm Formation in Vibrio fischeri
| Autor: | Karen L. Visick, Kati Geszvain |
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| Rok vydání: | 2008 |
| Předmět: |
Transcription
Genetic Blotting Western Molecular Sequence Data Microbiology Protein Structure Secondary Phosphotransferase Structure-Activity Relationship Bacterial Proteins PAS domain Gene cluster Aliivibrio fischeri Amino Acid Sequence Molecular Biology Models Genetic biology Phosphotransferases Histidine kinase Computational Biology Periplasmic space biology.organism_classification Protein Structure Tertiary Cell biology Transmembrane domain Biochemistry Biofilms Mutagenesis Site-Directed Signal transduction Signal Transduction |
| Zdroj: | Journal of Bacteriology. 190:4437-4446 |
| ISSN: | 1098-5530 0021-9193 |
| Popis: | Overexpression of the Vibrio fischeri sensor kinase RscS induces expression of the syp ( sy mbiosis p olysaccharide) gene cluster and promotes biofilm phenotypes such as wrinkled colony morphology, pellicle formation, and surface adherence. RscS is predicted to be a hybrid sensor kinase with a histidine kinase/ATPase (HATPase) domain, a receiver (Rec) domain, and a histidine phosphotransferase (Hpt) domain. Bioinformatic analysis also revealed the following three potential signal detection domains within RscS: two transmembrane helices forming a transmembrane region (TMR), a large periplasmic (PP) domain, and a cytoplasmic PAS domain. In this work, we genetically dissected the contributions of these domains to RscS function. Substitutions within the carboxy-terminal domain supported identification of RscS as a hybrid sensor kinase; disruption of both the HATPase and Rec domains eliminated induction of syp transcription, wrinkled colony morphology, pellicle formation, and surface adherence, while disruption of Hpt resulted in decreased activity. The PAS domain was also critical for RscS activity; substitutions in PAS resulted in a loss of activity. Generation of a cytoplasmic, N-terminal deletion derivative of RscS resulted in a partial loss of activity, suggesting a role for localization to the membrane and/or sequences within the TMR and PP domain. Finally, substitutions within the first transmembrane helix of the TMR and deletions within the PP domain both resulted in increased activity. Thus, RscS integrates both inhibitory and stimulatory signals from the environment to regulate biofilm formation by V. fischeri . |
| Databáze: | OpenAIRE |
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