ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structural asymmetry in a conserved signaling system that regulates division, replication, and virulence of an intracellular pathogen.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
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- Chromosomal gene of hybrid multisensor histidine kinase is involved in motility regulation in the rhizobacterium Azospirillum baldaniorum Sp245 under mechanical and water stress.World journal of microbiology & biotechnology · 2023Article
- TheAnnual review of microbiology · 2023Review
- Structural features discriminating hybrid histidine kinase Rec domains from response regulator homologs.Nature communications · 2023Article
- Genome-wide analysis of Brucella melitensis genes required throughout intranasal infection in mice.PLoS pathogens · 2022Article
- Combined immunization with inactivated vaccine reduces the dose of live B. abortus A19 vaccine.BMC veterinary research · 2022Article
- Hybrid Histidine Kinase WelA ofFrontiers in microbiology · 2022Article
- Uncovering the Hidden Credentials ofMicrobiology and molecular biology reviews : MMBR · 2021Review
- The CckA-ChpT-CtrA Phosphorelay Controlling Rhodobacter capsulatus Gene Transfer Agent Production Is Bidirectional and Regulated by Cyclic di-GMP.Journal of bacteriology · 2021Article
- Bacterial Protein Kinases.Advances in experimental medicine and biology · 2021Article
- Article
- Structural asymmetry does not indicate hemiphosphorylation in the bacterial histidine kinase CpxA.The Journal of biological chemistry · 2020Article
- Integrative and quantitative view of the CtrA regulatory network in a stalked budding bacterium.PLoS genetics · 2020Article
- Hybrid histidine kinase activation by cyclic di-GMP-mediated domain liberation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- DNA and Polyphosphate in Directed Proteolysis for DNA Replication Control.Frontiers in microbiology · 2020Review
- Bacterial cell cycle and growth phase switch by the essential transcriptional regulator CtrA.Nucleic acids research · 2019Article
- Structural basis for activation of a diguanylate cyclase required for bacterial predation in Bdellovibrio.Nature communications · 2019Article
- Article
- Periplasmic protein EipA determines envelope stress resistance and virulence in Brucella abortus.Molecular microbiology · 2019Article
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5 authors.
Funding
Abstract
We have functionally and structurally defined an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival of the global zoonotic pathogen Brucella abortus. Our study delineates phosphoryl transfer through this molecular pathway, which initiates from the sensor kinase CckA and proceeds through the ChpT phosphotransferase to two regulatory substrates: CtrA and CpdR. Genetic perturbation of this system results in defects in cell growth and division site selection, and a specific viability deficit inside human phagocytic cells. Thus, proper control of B. abortus division site polarity is necessary for survival in the intracellular niche. We further define the structural foundations of signaling from the central phosphotransferase, ChpT, to its response regulator substrate, CtrA, and provide evidence that there are at least two modes of interaction between ChpT and CtrA, only one of which is competent to catalyze phosphoryltransfer. The structure and dynamics of the active site on each side of the ChpT homodimer are distinct, supporting a model in which quaternary structure of the 2:2 ChpT-CtrA complex enforces an asymmetric mechanism of phosphoryl transfer between ChpT and CtrA. Our study provides mechanistic understanding, from the cellular to the atomic scale, of a conserved transcriptional regulatory system that controls the cellular and infection biology of B. abortus. More generally, our results provide insight into the structural basis of two-component signal transduction, which is broadly conserved in bacteria, plants, and fungi.
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