title: CheZ phosphatase localizes to chemoreceptor patches via CheA-short.
abstract: We have investigated the conditions required for polar localization of the CheZ phosphatase by using a CheZ-green fluorescent protein fusion protein that, when expressed from a single gene in the chromosome, restored chemotaxis to a DeltacheZ strain. Localization was observed in wild-type, DeltacheZ, DeltacheYZ, and DeltacheRB cells but not in cells with cheA, cheW, or all chemoreceptor genes except aer deleted. Cells making only CheA-short (CheA(S)) or CheA lacking the P2 domain also retained normal localization, whereas cells producing only CheA-long or CheA missing the P1 and P2 domains did not. We conclude that CheZ localization requires the truncated C-terminal portion of the P1 domain present in CheA(S). Missense mutations targeting residues 83 through 120 of CheZ also abolished localization. Two of these mutations do not disrupt chemotaxis, indicating that they specifically prevent interaction with CheA(S) while leaving other activities of CheZ intact.
authors.affiliation: Department of Biology, Texas A&M University, College Station, Texas 77843, USA.
authors.forename: Brian J
authors.initials: BJ
authors.lastname: Cantwell
authors.forename: Roger R
authors.initials: RR
authors.lastname: Draheim
authors.forename: Richard B
authors.initials: RB
authors.lastname: Weart
authors.forename: Cameran
authors.initials: C
authors.lastname: Nguyen
authors.forename: Richard C
authors.initials: RC
authors.lastname: Stewart
authors.forename: Michael D
authors.initials: MD
authors.lastname: Manson
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002628:Chemoreceptor Cells / Q000378:metabolism*; D002633:Chemotaxis / Q000235:genetics; D017124:Conserved Sequence; D004755:Enterobacteriaceae / Q000378:metabolism; D049452:Green Fluorescent Proteins; D057927:Hydrophobic and Hydrophilic Interactions; D008164:Luminescent Proteins / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013347:Subcellular Fractions
chemical_list: D001426:Bacterial Proteins; D008164:Luminescent Proteins; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins; D011494:Protein Kinases