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Chapter 31 : Chemotaxis and Motility

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Abstract:

Complete sequencing of bacterial and archaeal genomes has provided an opportunity to compare the chemotaxis machinery of and with that of other organisms and should give insight into what the ancestral mechanism might have been. Two major findings indicate that emerges as a model organism for the study of microbial chemotaxis. First, homologs of several chemotaxis proteins that are not present in are found in other bacterial and archaeal species. Second, the CheZ phosphatase, the only chemotaxis protein that is not present in , is missing from most other microbial genomes and thus may be of marginal importance. For peritrichous bacteria, chemotaxis occurs by modulating the tendency to rotate the flagella counterclockwise (CCW), for smooth swimming, or rotate them clockwise, for tumbling. The features of chemotaxis include the methyltransferase (CheR) (R), which uses S-adenosylmethionine (SAM) to catalyze methylesterification of particular glutamate residues in the receptor, and the methylesterase, CheB, which removes them. Motility gene expression in is absolutely dependent on σ, and motility is absolutely required for chemotaxis.

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31

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Bacteria and Archaea
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Gene Expression and Regulation
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Figures

Image of FIGURE 1
FIGURE 1

Time course of addition and removal of attractant to ( ). Cells are sheared so that a fragment of a flagellum remains, and this is tethered to a glass coverslip using anti-flagellar antibody. Owing to rotation of the flagellar fragment, the cell body rotates. The coverslip is made to form the ceiling of a laminar flow chamber, and buffer, with or without attractants, is flowed through the chamber; the cell rotation is followed as a function of time using videomicroscopy. Later, the time courses of a number of cells are averaged to give the probability of counterclockwise (CCW) rotation of the flagellum, which corresponds to smooth swimming. “Excitation” refers to addition of attractant; “de-excitation” refers to removal of attractant.

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31
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Image of FIGURE 2
FIGURE 2

Diagram of mechanism of chemotaxis in . A view of the reactions that occur during chemotaxis to asparagine mediated by McpB, the sole asparagine receptor, is shown. These features include the autophosphorylation of the kinase (CheA) (A), which is accelerated by addition of attractant, and the subsequent phosphoryl transfer to the main response regulator (CheY) (Y), the methylesterase (CheB) (B), and the coupling protein (CheV) (V). Subsequently, CheY-P binds to the switch to cause counterclockwise (CCW) rotation. The features also include the methyltransferase (CheR) (R), which uses S-adenosylmethionine (SAM) to catalyze methylesterification of particular glutamate residues in the receptor, and the methylesterase, CheB, which removes them. The diagram also includes the coupling protein CheW (W) and two regulatory proteins, CheC (C) and CheD (D). See text for details.

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31
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Image of FIGURE 3
FIGURE 3

Diagram of receptor structure in . The receptors are transmembrane proteins that are almost exclusively alpha helix. The “sensing domain” refers to the extracellular region where attractant is thought to bind. The “transmembrane helices” refer to where the sensing extracellular N-terminal region joins the information-processing C-terminal region. The “methylation region” refers to the region where methylation of specific glutamate residues occurs, usually to facilitate adaptation to stimulus. The “signaling region” refers to where the kinase (CheA) and coupling proteins (CheW and CheV) occur in order to bring about excitation or deexcitation.

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31
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Image of FIGURE 4
FIGURE 4

Class I, II, and III receptors. The three classes of receptors are distinguished by the number of “inserted” pairs of 14 amino acids (“INDELs”; see text), which are four turns of alpha helix; these are shaded. Class I receptors, found in many eubacteria, such as , have none. Class II receptors, found in other eubacteria, have one set, in the signaling region (see Fig. 3 ). Class III receptors, found in the low-G+C gram-positive organisms and the archaea, have two sets—one in the signaling region and the other in the methylation region. Sites of methylation based on the consensus site for an example of each class are indicated. See reference for more details.

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31
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Image of FIGURE 5
FIGURE 5

Time course effect of addition of 504 μΜ asparagine to wild-type , a mutant having , and a mutant having . Thick line, wild type; medium line, mutant; thin line, CCW, counterclockwise. Adapted from Zimmer et al. ( ) with permission of the American Society for Biochemistry and Molecular Biology.

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31
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Image of FIGURE 6
FIGURE 6

Diagram of hypothesized forces and conformations of McpB upon addition or removal of asparagine when sites 630 and 637 of McpB of are methylated selectively. The negative charge between sites 630 and 637 of one monomer might be on the other monomer or on an associated protein. Initial binding of asparagine causes upward movement of the second transmembrane helix of one monomer of the dimer. Adaptation occurs upon changes in which residues in that same monomer are methylated and results from charge-charge repulsion causing a vertical interdimeric force in the opposite direction from that before the methylation changes. Conversely, removal of asparagine causes a downward movement of the second transmembrane helix of the same monomer, and adaptation results from changing back to the prestimulus distribution of methyl groups. Reprinted from Zimmer et al. ( ) with permission of the American Society for Biochemistry and Molecular Biology.

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31
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Image of FIGURE 7
FIGURE 7

Phylogenetic trees of selected chemotaxis proteins. The trees were built from multiple sequence alignments constructed by using the CLUSTAL X program ( ). Two major clusters are apparent: (i) gram-positive bacteria, archaea, and spirochaeta (in bold) and (ii) proteobacteria. Abbreviations: Aful, ; Atum, ; Bbro, ; Bbur, ; Bper, ; Bste, ; Bsub, ; Cace, ; Ccre, ; Cdif, ; Cjej, ; Ecol, ; Hpyl, ; Hsal, ; Lmon, ; Paby, ; Paer, ; Phor, ; Pput, ; Rcen, ; Rsph, ; Smel, ; Styp, ; Tden, ; Tmar, ; Tpal, ; Vcho, .

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31
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Image of FIGURE 8
FIGURE 8

A phylogenetic tree of CheC and related proteins. The tree was built from a multiple sequence alignment constructed by using the CLUSTAL X program ( ). FliY and FliM indicate CheC-like domains from the corresponding proteins that have been extracted and included in the alignment. Clusters of CheC and CheX proteins are in bold. Abbreviations: Sput, ; Styphi, ; Vpar, ; Ypes, . See the legend to Fig. 7 for other species abbreviations.

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31
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Image of FIGURE 9
FIGURE 9

Electron micrographs of flagella in various forms ( ). (A) Cell with flagella. (B) Intact flagella from . Bar represents 100 nm. (C) Hook-basal body (HBB) of . HBBs were purified as follows: bacteria were grown at 37°C to late exponential phase and suspended in sucrose solution (0.5 Μ sucrose, 0.15 Μ Trizma base; pH not adjusted) containing 1 mM protease inhibitor. Lysozyme and then Triton X-100 and, after a drop in viscosity, 10 mM EDTA were added to prevent reaggregation of cell membranes and walls. To remove membrane proteins, the pH of the solution was raised up to 10 by adding drops of 1 ? NaOH solution. After sedimentation in a 33% (wt/vol) CsCl gradient, intact flagella were recovered from a band in the middle of the centrifuge tube, washed with water, and resuspended in ?ΕΤ (10 mM Tris-HCl, pH 8; 1 mM EDTA, 0.1% Triton X-100). The filament part of the flagella was dissociated in 50 mM glycine buffer (pH 3.0) at room temperature for 1 h. A lower pH value (pH 2.5) used for enterica serovar Typhimurium resulted in partial degradation of the hook and the rod. Bar represents 100 nm. (D) Partially isolated flagella that retained the C ring at the basal body. Negatively stained with 2% phosphotungstic acid (pH 4.0).

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31
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Image of FIGURE 10
FIGURE 10

Diagram of HBB complexes of and serovar Typhimurium

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31
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Image of FIGURE 11
FIGURE 11

Chromosomal map of (4.2 Mbp), indicating motility and related genes. The genes from to are in the “major / operon.”

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31
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Tables

Generic image for table
TABLE 1

Specificities of receptors of

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31
Generic image for table
TABLE 2

Properties of chemotaxis proteins of

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31
Generic image for table
TABLE 3

Comparisons of flagellar gene-protein-substructure relationships in and serovar Typhimurium

Apparent molecular mass as measured by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

Amino acid sequence homology using SIM Alignment Tool for protein with these parameters: number of alignments to be computed, 10; gap open penalty, 8; gap extension penalty, 0; comparison matrix, BLOSOM30.

Speculation on unknown gene product deduced from homology search; proposed new name and function need experimental verification.

MinD ()is not a flagellar protein, but it may affect the efficiency of flagellation.

Citation: Aizawa S, Zhulin I, Márquez-Magaña L, Ordal G. 2002. Chemotaxis and Motility, p 437-452. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch31

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