title: Dynamic Clustering of the Bacterial Sensory Kinase BaeS.
abstract: Several bacterial sensory-kinase receptors form clusters on the cell membrane. However, the dynamics of sensory-kinase clustering are largely unclear. Using measurements of fluorescence anisotropy and time-lapse imaging of Escherichia coli cells, we demonstrate that copper ions trigger self-association of BaeS receptors and lead to rapid formation of clusters, which can be reversibly dispersed by a metal chelator. Copper ions did not trigger self-association of other fluorescently tagged sensory kinases, and other divalent metal ions could not elicit self-association of BaeS. The histidine residues in the BaeS periplasmic domain are essential for copper binding in vitro and are important for the copper-induced BaeS responses in vivo. BaeS clustering was triggered also under conditions that directly triggered BaeS-dependent transcriptional responses. Thus, clustering of sensory kinase receptors can be dynamic and context dependent and can be triggered by specific environmental cues.
authors.affiliation: The Racah Institute of Physics, The Hebrew University of Jerusalem, Safra Campus, Givat Ram, Jerusalem, 91904, Israel.
authors.forename: Moriah
authors.initials: M
authors.lastname: Koler
authors.affiliation: The Racah Institute of Physics, The Hebrew University of Jerusalem, Safra Campus, Givat Ram, Jerusalem, 91904, Israel.
authors.forename: Vered
authors.initials: V
authors.lastname: Frank
authors.affiliation: The Institute of Chemistry, The Hebrew University of Jerusalem, Safra Campus, Givat Ram, Jerusalem, 91904, Israel.
authors.forename: Hadar
authors.initials: H
authors.lastname: Amartely
authors.affiliation: The Institute of Chemistry, The Hebrew University of Jerusalem, Safra Campus, Givat Ram, Jerusalem, 91904, Israel.
authors.forename: Assaf
authors.initials: A
authors.lastname: Friedler
authors.affiliation: The Racah Institute of Physics, The Hebrew University of Jerusalem, Safra Campus, Givat Ram, Jerusalem, 91904, Israel.
authors.forename: Ady
authors.initials: A
authors.lastname: Vaknin
mesh_terms: D003300:Copper / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D004347:Drug Interactions; D004926:Escherichia coli / Q000166:cytology* / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006639:Histidine; D006863:Hydrogen-Ion Concentration; D009154:Mutation; D019897:Periplasm / Q000187:drug effects / Q000378:metabolism; D033903:Periplasmic Proteins / Q000235:genetics; D011401:Promoter Regions, Genetic / Q000235:genetics; D011494:Protein Kinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D014158:Transcription, Genetic / Q000187:drug effects; D017973:Tungsten Compounds / Q000494:pharmacology
chemical_list: D029968:Escherichia coli Proteins; D033903:Periplasmic Proteins; C104888:Spy protein, E coli; D017973:Tungsten Compounds; D006639:Histidine; C025399:sodium tungstate(VI); D003300:Copper; D011494:Protein Kinases; C583423:BaeS protein, E coli