In molecular biology, the flagellar motor switch protein(Flig) is one of
three proteins in certain
bacteria coded for by the gene fliG.[1] The other two
proteins are FliN coded for by fliN,[2] and FliM coded for by fliM.[3] The
protein complex regulates the direction of
flagellar rotation and hence controls swimming behaviour.[4] The switch is a complex apparatus that responds to
signals transduced by the
chemotaxis sensory signalling system during chemotactic behaviour.[4] CheY, the chemotaxis response regulator, is believed to act directly on the switch to induce a switch in the flagellar motor direction of rotation.
Fli proteins
The switch complex comprises at least three
proteins - FliG, FliM and FliN.[2] It has been shown that FliG
interacts with FliM, FliM
interacts with itself, and FliM interacts with FliN.[5] Several
amino acids within the middle third of FliG appear to be strongly involved in the FliG-FliM interaction, with residues near the
N- or
C-termini being less important.[5] Such clustering suggests that FliG-FliM interaction plays a central role in switching.
Analysis of the FliG, FliM and FliN
sequences shows that none are especially
hydrophobic or appear to be
integral membrane proteins.[6] This result is consistent with other evidence suggesting that the
proteins may be
peripheral to the membrane, possibly mounted on the
basal body M ring.[6][7] FliG is present in about 25 copies per
flagellum. The
structure of the C-terminal
domain of FliG is known, this domain functions specifically in motor rotation.[8]
^
abRoman SJ, Frantz BB, Matsumura P (October 1993). "Gene sequence, overproduction, purification and determination of the wild-type level of the Escherichia coli flagellar switch protein FliG". Gene. 133 (1): 103–8.
doi:
10.1016/0378-1119(93)90232-R.
PMID8224881.
In molecular biology, the flagellar motor switch protein(Flig) is one of
three proteins in certain
bacteria coded for by the gene fliG.[1] The other two
proteins are FliN coded for by fliN,[2] and FliM coded for by fliM.[3] The
protein complex regulates the direction of
flagellar rotation and hence controls swimming behaviour.[4] The switch is a complex apparatus that responds to
signals transduced by the
chemotaxis sensory signalling system during chemotactic behaviour.[4] CheY, the chemotaxis response regulator, is believed to act directly on the switch to induce a switch in the flagellar motor direction of rotation.
Fli proteins
The switch complex comprises at least three
proteins - FliG, FliM and FliN.[2] It has been shown that FliG
interacts with FliM, FliM
interacts with itself, and FliM interacts with FliN.[5] Several
amino acids within the middle third of FliG appear to be strongly involved in the FliG-FliM interaction, with residues near the
N- or
C-termini being less important.[5] Such clustering suggests that FliG-FliM interaction plays a central role in switching.
Analysis of the FliG, FliM and FliN
sequences shows that none are especially
hydrophobic or appear to be
integral membrane proteins.[6] This result is consistent with other evidence suggesting that the
proteins may be
peripheral to the membrane, possibly mounted on the
basal body M ring.[6][7] FliG is present in about 25 copies per
flagellum. The
structure of the C-terminal
domain of FliG is known, this domain functions specifically in motor rotation.[8]
^
abRoman SJ, Frantz BB, Matsumura P (October 1993). "Gene sequence, overproduction, purification and determination of the wild-type level of the Escherichia coli flagellar switch protein FliG". Gene. 133 (1): 103–8.
doi:
10.1016/0378-1119(93)90232-R.
PMID8224881.