WebMay 29, 2024 · U.S. Department of Energy Office of Scientific and Technical Information. Search Scholarly Publications. Search terms: Advanced search options In molecular biology, the flagellar motor switch protein (Flig) is one of three proteins in certain bacteria coded for by the gene fliG. The other two proteins are FliN coded for by fliN, and FliM coded for by fliM. The protein complex regulates the direction of flagellar rotation and hence controls swimming behaviour. The switch is a complex apparatus that responds to signals transduced by the chemotaxis sensory signalling system during chemotactic behaviour. CheY, the chemotaxi…

Signal-dependent turnover of the bacterial flagellar …

WebFLAGELLAR MOTOR SWITCH PROTEIN FLIM. NCBI. National Center for Biotechnology Information. Search. 4FHR: Crystal Structure Of The Complex Between The Flagellar Motor Proteins Flig And Flim. PDB ID: 4FHR Download: MMDB ID: 102194: PDB Deposition Date: 2012/6/6: Updated in MMDB: 2012/11: Experimental Method: x-ray … WebMar 3, 2024 · IMPORTANCE The bacterial flagellar motor is an ultrasensitive motor. Its output, the probability of the motor turning clockwise, depends sensitively on the occupancy of the protein FliM (a component on the switch complex of the motor) by the input CheY-P molecules. With a limited cellular pool of CheY-P molecules, cell-to-cell variation of the ... coz investors llc

Molecular mechanism for rotational switching of the …

Webflagellar motor switch protein FliM; Members of this family are the flagellar motor switch protein FliM. The family excludes FliM homologs that lack an N-terminal region critical to interaction with phosphorylated CheY. One set lacking this N-terminal region is found in Rhizobium meliloti, in which the direction of flagellar rotation is not ... WebOct 25, 2005 · FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. A high-passage B. burgdorferi sensu stricto strain B31A (WT) and its isogenic mutants were grown in Barbour–Stoenner–Kelly II (BSK-II) liquid medium or on semisolid agar plates at 34 °C in the presence of 3.4% carbon dioxide as previously described13,37. Escherichia coli TOP10 strain (Invitrogen) was used for DNA … See more The vectors for in-frame replacement of cheX-cheY3 with cheY3-gfp were constructed by using a PCR-based fusion method, as previously described38. Briefly, the PCR primers (containing complementary … See more Fluorescence images of cheX::cheY3-GFP B. burgdorfericells were taken using a Zeiss Axiostar plus microscope at a wavelength of 480 nm. The images were captured and processed using the program ZEN (Zeiss). See more Site-directed mutagenesis was performed using QuikChange site-directed mutagenesis kit (Stratagene) according to the manufacturer’s instructions. The above-constructed cheY3 pGEM-T Easy vector was used as a … See more The full-length cheY3 or cheY3* genes were used (in cheY3*, Asp 79, a key residue required for the phosphorylation, was replaced by Ala (Table 1)). The cheY3 gene was first … See more cozio defense