Journal article
Chemosensory regulation of a HEAT-repeat protein couples aggregation and sporulation in Myxococcus xanthus
Journal of bacteriology, Vol.196(17), pp.3160-3168
09/2014
DOI: 10.1128/JB.01866-14
PMCID: PMC4135651
PMID: 24957622
Abstract
Chemosensory systems are complex, highly modified two-component systems (TCS) used by bacteria to control various biological functions ranging from motility to sporulation. Chemosensory systems and TCS both modulate phosphorelays comprised of histidine kinases and response regulators, some of which are single-domain response regulators (SD-RRs) such as CheY. In this study, we have identified and characterized the Che7 chemosensory system of Myxococcus xanthus, a common soil bacterium which displays multicellular development in response to stress. Both genetic and biochemical analyses indicate that the Che7 system regulates development via a direct interaction between the SD-RR CheY7 and a HEAT repeat domain-containing protein, Cpc7. Phosphorylation of the SD-RR affects the interaction with its target, and residues within the α4-β5-α5 fold of the REC domain govern this interaction. The identification of the Cpc7 interaction with CheY7 extends the diversity of known targets for SD-RRs in biological systems.
Details
- Title: Subtitle
- Chemosensory regulation of a HEAT-repeat protein couples aggregation and sporulation in Myxococcus xanthus
- Creators
- Cynthia L Darnell - Department of Microbiology, University of Iowa, Iowa City, Iowa, USAJanet M Wilson - Division of Select Agents and Toxins, Office of Public Health Preparedness and Response, Centers for Disease Control and Prevention, Atlanta, Georgia, USANitija Tiwari - Department of Biochemistry, University of Iowa, Iowa City, Iowa, USAErnesto J Fuentes - Department of Biochemistry, University of Iowa, Iowa City, Iowa, USAJohn R Kirby - Department of Microbiology, University of Iowa, Iowa City, Iowa, USA john-kirby@uiowa.edu
- Resource Type
- Journal article
- Publication Details
- Journal of bacteriology, Vol.196(17), pp.3160-3168
- Publisher
- United States
- DOI
- 10.1128/JB.01866-14
- PMID
- 24957622
- PMCID
- PMC4135651
- ISSN
- 0021-9193
- eISSN
- 1098-5530
- Grant note
- T32 GM008365 / NIGMS NIH HHS
- Language
- English
- Date published
- 09/2014
- Academic Unit
- Biochemistry and Molecular Biology
- Record Identifier
- 9984024517502771
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