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Histidine kinase regulation by a cyclophilin-like inhibitor.

Jacques DA, Langley DB, Jeffries CM, Cunningham KA, Burkholder WF, Guss JM, Trewhella J
J Mol Biol 384 422-35 (2008)
Cited: 22 times
EuropePMC logo PMID: 18823995

Abstract

The sensor histidine kinase A (KinA) from Bacillus subtilis triggers a phosphorelay that activates sporulation. The antikinase KipI prevents sporulation by binding KinA and inhibiting the autophosphorylation reaction. Using neutron contrast variation, mutagenesis, and fluorescence data, we show that two KipI monomers bind via their C-domains at a conserved proline in the KinA dimerization and histidine-phosphotransfer (DHp) domain. Our crystal structure of the KipI C-domain reveals the binding motif has a distinctive hydrophobic groove formed by a five-stranded antiparallel beta-sheet; a characteristic of the cyclophilin family of proteins that bind prolines and often act as cis-trans peptidyl-prolyl isomerases. We propose that the DHp domain of KinA transmits conformational signals to regulate kinase activity via this proline-mediated interaction. Given that both KinA and KipI homologues are widespread in the bacterial kingdom, this mechanism has broad significance in bacterial signal transduction.

Reviews - 2zp2 mentioned but not cited (1)

  1. Diversity in Sensing and Signaling of Bacterial Sensor Histidine Kinases. Ishii E, Eguchi Y. Biomolecules 11 1524 (2021)

Articles - 2zp2 mentioned but not cited (1)

  1. Crystal structure of urea carboxylase provides insights into the carboxyltransfer reaction. Fan C, Chou CY, Tong L, Xiang S. J Biol Chem 287 9389-9398 (2012)


Reviews citing this publication (7)

  1. Recent progress in Bacillus subtilis sporulation. Higgins D, Dworkin J. FEMS Microbiol Rev 36 131-148 (2012)
  2. Bacterial sensor kinases: diversity in the recognition of environmental signals. Krell T, Lacal J, Busch A, Silva-Jiménez H, Guazzaroni ME, Ramos JL. Annu Rev Microbiol 64 539-559 (2010)
  3. Small-angle scattering for structural biology--expanding the frontier while avoiding the pitfalls. Jacques DA, Trewhella J. Protein Sci 19 642-657 (2010)
  4. Determinants of specificity in two-component signal transduction. Podgornaia AI, Laub MT. Curr Opin Microbiol 16 156-162 (2013)
  5. Three (and more) component regulatory systems - auxiliary regulators of bacterial histidine kinases. Buelow DR, Raivio TL. Mol Microbiol 75 547-566 (2010)
  6. Structural Insights into High Density Lipoprotein: Old Models and New Facts. Gogonea V. Front Pharmacol 6 318 (2015)
  7. Genetic mechanisms governing sporulation initiation in Clostridioides difficile. Lee CD, Rizvi A, Edwards AN, DiCandia MA, Vargas Cuebas GG, Monteiro MP, McBride SM. Curr Opin Microbiol 66 32-38 (2022)

Articles citing this publication (13)

  1. Full-length structure of a monomeric histidine kinase reveals basis for sensory regulation. Rivera-Cancel G, Ko WH, Tomchick DR, Correa F, Gardner KH. Proc Natl Acad Sci U S A 111 17839-17844 (2014)
  2. The histidine kinase inhibitor Sda binds near the site of autophosphorylation and may sterically hinder autophosphorylation and phosphotransfer to Spo0F. Cunningham KA, Burkholder WF. Mol Microbiol 71 659-677 (2009)
  3. In vivo domain-based functional analysis of the major sporulation sensor kinase, KinA, in Bacillus subtilis. Eswaramoorthy P, Guo T, Fujita M. J Bacteriol 191 5358-5368 (2009)
  4. prhKLM genes of Ralstonia solanacearum encode novel activators of hrp regulon and are required for pathogenesis in tomato. Zhang Y, Kiba A, Hikichi Y, Ohnishi K. FEMS Microbiol Lett 317 75-82 (2011)
  5. Mechanism of activation of PhoQ/PhoP two-component signal transduction by SafA, an auxiliary protein of PhoQ histidine kinase in Escherichia coli. Ishii E, Eguchi Y, Utsumi R. Biosci Biotechnol Biochem 77 814-819 (2013)
  6. A novel structure of an antikinase and its inhibitor. Jacques DA, Langley DB, Hynson RM, Whitten AE, Kwan A, Guss JM, Trewhella J. J Mol Biol 405 214-226 (2011)
  7. Novel modulators controlling entry into sporulation in Bacillus subtilis. Garti-Levi S, Eswara A, Smith Y, Fujita M, Ben-Yehuda S. J Bacteriol 195 1475-1483 (2013)
  8. The enigma of cytosolic two-component systems: a hypothesis. Krell T, Busch A, Lacal J, Silva-Jiménez H, Ramos JL. Environ Microbiol Rep 1 171-176 (2009)
  9. Role of the PAS sensor domains in the Bacillus subtilis sporulation kinase KinA. Winnen B, Anderson E, Cole JL, King GF, Rowland SL. J Bacteriol 195 2349-2358 (2013)
  10. Evidence that Autophosphorylation of the Major Sporulation Kinase in Bacillus subtilis Is Able To Occur in trans. Devi SN, Kiehler B, Haggett L, Fujita M. J Bacteriol 197 2675-2684 (2015)
  11. A new role for SR1 from Bacillus subtilis: regulation of sporulation by inhibition of kinA translation. Ul Haq I, Brantl S, Müller P. Nucleic Acids Res 49 10589-10603 (2021)
  12. 1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis. Hynson RM, Kwan AH, Jacques DA, Mackay JP, Trewhella J. Biomol NMR Assign 4 167-169 (2010)
  13. The Histidine Kinase CckA Is Directly Inhibited by a Response Regulator-like Protein in a Negative Feedback Loop. Vega-Baray B, Domenzain C, Poggio S, Dreyfus G, Camarena L. mBio 13 e0148122 (2022)


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