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CHEMOTAXIS-GUIDED MOVEMENTS IN BACTERIA
Renate Lux and
Wenyuan Shi*
School of Dentistry, Department of Microbiology, Immunology and Molecular Genetics, University of California-Los Angeles, Los Angeles, CA 90095;
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Figure 1. Original drawing from Antony van Leeuwenhoek’s notes. Shown are some types of bacteria that he observed in a dental plaque sample. Among them appear to be cocci (E), fusiforme bacteria (F), and spirochetes (G)
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Figure 2. Schematic illustration of basic chemotactic signal transduction pathway. The proteins involved in the basic chemotactic signal transduction pathway are shown. The excitation response involves signal reception by the chemoreceptors (MCP) and further signal transduction via CheW, CheA, and CheY to the flagella motor. Adaptation is achieved via methylation/demethylation of the MCPs by CheR and CheB. See text for details.
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Figure 3. Schematic illustration of chemoreceptor structure. The ‘classic’ chemoreceptor consists of an extracytoplasmic (periplasmic) ligand-binding domain and a transmembrane portion that connects to the cytoplasmic domain via a HAMP domain. The cytoplasmic domain contains the CheA/CheW binding domain and methylation sites that are substrate for CheR and CheB. See text for more details.
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Figure 4. Schematic illustration of CheA domain organization. CheA is organized into five distict domains: (a) a phosphotransfer domain (HPt), a response regulator binding domain (YB), a dimerization domain (D), a catalytic kinase domain (CA), and a chemoreceptor/CheW binding domain (R). (b) CheA forms a homodimer with the two subunits phosphorylating each other.
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Figure 5. Schematic illustration of flagella motor. The basic elements of the flagella rotary motor are shown. The basal body is formed by the membrane integral M/S-ring and its cytoplasmic extension, the C-ring, and connects via a curved hook to the flagellum. These parts are thought to comprise the rotary part of the flagella motor. The membrane-spanning Mot complexes build the stator that allows for torque generation. For more detailed information on architecture and function, see Macnab (1996, 1999).
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Critical Reviews in Oral Biology & Medicine, Vol. 15, No. 4,
207-220 (2004)
DOI: 10.1177/154411130401500404
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