ArticleMicrobiologyOpen2013
The cytoplasmic PASC domain of the sensor kinase DcuS of Escherichia coli: role in signal transduction, dimer formation, and DctA interaction.
Article in MicrobiologyOpen, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 33 citations in OpenAlex.
- Mechanism of sensor kinase CitA transmembrane signaling.Nature communications · 2025Article
- A signaling complex of adenylate cyclase CyaC of Sinorhizobium meliloti with cAMP and the transcriptional regulators Clr and CycR.BMC microbiology · 2023Article
- Article
- Conversion of the Sensor Kinase DcuS to the Fumarate Sensitive State by Interaction of the Bifunctional Transporter DctA at the TM2/PASMicroorganisms · 2021Article
- Structural insight into the role of the PAS domainfor signal transduction in sensor-kinase BvgS.Journal of bacteriology · 2021Article
- Phosphoregulated orthogonal signal transduction in mammalian cells.Nature communications · 2020Article
- Protein Activity Sensing in Bacteria in Regulating Metabolism and Motility.Frontiers in microbiology · 2019Review
- Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- C4-Dicarboxylate Utilization in Aerobic and Anaerobic Growth.EcoSal Plus · 2016Article
- Transmembrane signaling in the sensor kinase DcuS of Escherichia coli: A long-range piston-type displacement of transmembrane helix 2.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Characterization of mutations in the PAS domain of the EvgS sensor kinase selected by laboratory evolution for acid resistance in Escherichia coli.Molecular microbiology · 2014Article
- Mutational analysis of dimeric linkers in peri- and cytoplasmic domains of histidine kinase DctB reveals their functional roles in signal transduction.Open biology · 2014Article
- Multi-PAS domain-mediated protein oligomerization of PpsR from Rhodobacter sphaeroides.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Transmembrane signaling and cytoplasmic signal conversion by dimeric transmembrane helix 2 and a linker domain of the DcuS sensor kinase.The Journal of biological chemistryArticle
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5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The cytoplasmic PASC domain of the fumarate responsive sensor kinase DcuS of Escherichia coli links the transmembrane to the kinase domain. PASC is also required for interaction with the transporter DctA serving as a cosensor of DcuS. Earlier studies suggested that PASC functions as a hinge and transmits the signal to the kinase. Reorganizing the PASC dimer interaction and, independently, removal of DctA, converts DcuS to the constitutive ON state (active without fumarate stimulation). ON mutants were categorized with respect to these two biophysical interactions and the functional state of DcuS: type I-ON mutations grossly reorganize the homodimer, and decrease interaction with DctA. Type IIA-ON mutations create the ON state without grossly reorganizing the homodimer, whereas interaction with DctA is decreased. The type IIB-ON mutations were neither in PASC /PASC , nor in DctA/DcuS interaction affected, similar to fumarate activated wild-typic DcuS. OFF mutations never affected dimer stability. The ON mutations provide novel mechanistic insight: PASC dimerization is essential to silence the kinase. Reorganizing the homodimer and its interaction with DctA activate the kinase. The study suggests a novel ON homo-dimer conformation (type IIB) and an OFF conformation for PASC . Type IIB-ON corresponds to the fumarate induced wild-type conformation, representing an interesting target for structural biology.
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