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Chemosensory regulation of a HEAT-repeat protein couples aggregation and sporulation in Myxococcus xanthus. J Bacteriol 2014 Sep;196(17):3160-8

Date

06/25/2014

Pubmed ID

24957622

Pubmed Central ID

PMC4135651

DOI

10.1128/JB.01866-14

Scopus ID

2-s2.0-84905472288 (requires institutional sign-in at Scopus site)   8 Citations

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.

Author List

Darnell CL, Wilson JM, Tiwari N, Fuentes EJ, Kirby JR

Author

John Kirby PhD Chair, Center Associate Director, Professor in the Microbiology and Immunology department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Bacterial Proteins
Gene Expression Regulation, Bacterial
Molecular Sequence Data
Multigene Family
Myxococcus xanthus
Phylogeny
Protein Binding
Protein Conformation
Spores, Bacterial