ArticleThe Journal of biological chemistry2009
A novel "four-component" two-component signal transduction mechanism regulates developmental progression in Myxococcus xanthus.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 41 citations in OpenAlex.
- Article
- General strategies for using amino acid sequence data to guide biochemical investigation of protein function.Biochemical Society transactions · 2022Review
- Modulation of Response Regulator CheY Reaction Kinetics by Two Variable Residues That Affect Conformation.Journal of bacteriology · 2020Article
- New Insights into Multistep-Phosphorelay (MSP)/ Two-Component System (TCS) Regulation: Are Plants and Bacteria that Different?Plants (Basel, Switzerland) · 2019Review
- Orphan Hybrid Histidine Protein Kinase SinK Acts as a Signal Integrator To Fine-Tune Multicellular Behavior inJournal of bacteriology · 2019Article
- Article
- The ChrSA and HrrSA Two-Component Systems Are Required for Transcriptional Regulation of the hemA Promoter in Corynebacterium diphtheriae.Journal of bacteriology · 2016Article
- Two-Component Signal Transduction Systems That Regulate the Temporal and Spatial Expression of Myxococcus xanthus Sporulation Genes.Journal of bacteriology · 2016Review
- Chemosensory regulation of a HEAT-repeat protein couples aggregation and sporulation in Myxococcus xanthus.Journal of bacteriology · 2014Article
- Structural basis of a rationally rewired protein-protein interface critical to bacterial signaling.Structure (London, England : 1993) · 2013Article
- Domain analysis of ArcS, the hybrid sensor kinase of the Shewanella oneidensis MR-1 Arc two-component system, reveals functional differentiation of its two receiver domains.Journal of bacteriology · 2013Article
- Intra- and interprotein phosphorylation between two-hybrid histidine kinases controls Myxococcus xanthus developmental progression.The Journal of biological chemistry · 2012Article
- Multiple orphan histidine kinases interact directly with Spo0A to control the initiation of endospore formation in Clostridium acetobutylicum.Molecular microbiology · 2011Article
- Article
- The genetic organisation of prokaryotic two-component system signalling pathways.BMC genomics · 2010Article
- ArcS, the cognate sensor kinase in an atypical Arc system of Shewanella oneidensis MR-1.Applied and environmental microbiology · 2010Article
- Global transcriptome analysis of spore formation in Myxococcus xanthus reveals a locus necessary for cell differentiation.BMC genomics · 2010Article
- Receiver domain structure and function in response regulator proteins.Current opinion in microbiology · 2010Review
- How important is the phosphatase activity of sensor kinases?Current opinion in microbiology · 2010Review
- Matching biochemical reaction kinetics to the timescales of life: structural determinants that influence the autodephosphorylation rate of response regulator proteins.Journal of molecular biology · 2009Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Histidine-aspartate phosphorelays are employed by two-component signal transduction family proteins to mediate responses to specific signals or stimuli in microorganisms and plants. The RedCDEF proteins constitute a novel signaling system in which four two-component proteins comprising a histidine kinase, a histidine-kinase like protein, and two response regulators function together to regulate progression through the elaborate developmental program of Myxococcus xanthus. A combination of in vivo phenotypic analyses of in-frame deletions and non-functional point mutations in each gene as well as in vitro autophosphorylation and phosphotransfer analyses of recombinant proteins indicate that the RedC histidine kinase protein autophosphorylates and donates a phosphoryl group to the single domain response regulator, RedF, to repress progression through the developmental program. To relieve this developmental repression, RedC instead phosphorylates RedD, a dual receiver response regulator protein. Surprisingly, RedD transfers the phosphoryl group to the histidine kinase-like protein RedE, which itself appears to be incapable of autophosphorylation. Phosphorylation of RedE may render RedE accessible to RedF, where it removes the phosphoryl group from RedF-P, which is otherwise an unusually stable phosphoprotein. These analyses reveal a novel "four-component" signaling mechanism that has probably arisen to temporally coordinate signals controlling the developmental program in M. xanthus. The RedCDEF signaling system provides an important example of how the inherent plasticity and modularity of the basic two-component signaling domains comprise a highly adaptable framework well suited to expansion into complex signaling mechanisms.
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