Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis

Hess, Judith; Oosawa, Kenji; Kaplan, Nachum; Simon, Melvin I.

doi:10.1016/0092-8674(88)90489-8

Cited by 563 publications

(525 citation statements)

References 26 publications

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“…In E. coli (Fig. 1a), it is accelerated by a protein (CheZ) that functionally is a phosphatase : CheZ, by binding to free CheY-P, effectively accelerates its dephosphorylation (Bren et al, 1996 ;Hess et al, 1988). S. meliloti (Fig.…”

Section: Signalling Pathwaysmentioning

confidence: 99%

Sinorhizobial chemotaxis: a departure from the enterobacterial paradigm a aTo Professor Wolfram Heumann on his 87th birthday.

Schmitt

2002

Microbiology

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Section: Signalling Pathwaysmentioning

confidence: 99%

Sinorhizobial chemotaxis: a departure from the enterobacterial paradigm a aTo Professor Wolfram Heumann on his 87th birthday.

Schmitt

2002

Microbiology

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“…They concluded from these data that the chemotactic signal is inactivated as it diffuses through the cytoplasm, decreasing in strength by one-third every 2 m (28). The mediator of this signal was subsequently shown to be CheY-P (13,32), which undergoes dephosphorylation as it diffuses through the cytoplasm. In an elongated filamentous cell, it is unlikely that CheY-P from the cell poles reaches flagella all along the cell body.…”

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confidence: 99%

Motility and Chemotaxis of Filamentous Cells of Escherichia coli

Maki¹,

Gestwicki²,

Lake³

et al. 2000

J Bacteriol

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Filamentous cells of Escherichia coli can be produced by treatment with the antibiotic cephalexin, which blocks cell division but allows cell growth. To explore the effect of cell size on chemotactic activity, we studied the motility and chemotaxis of filamentous cells. The filaments, up to 50 times the length of normal E. coli organisms, were motile and had flagella along their entire lengths. Despite their increased size, the motility and chemotaxis of filaments were very similar to those properties of normal-sized cells. Unstimulated filaments of chemotactically normal bacteria ran and stopped repeatedly (while normal-sized bacteria run and tumble repeatedly). Filaments responded to attractants by prolonged running (like normal-sized bacteria) and to repellents by prolonged stopping (unlike normal-sized bacteria, which tumble), until adaptation restored unstimulated behavior (as occurs with normal-sized cells). Chemotaxis mutants that always ran when they were normal sized always ran when they were filament sized, and those mutants that always tumbled when they were normal sized always stopped when they were filament sized. Chemoreceptors in filaments were localized to regions both at the poles and at intervals along the filament. We suggest that the location of the chemoreceptors enables the chemotactic responses observed in filaments. The implications of this work with regard to the cytoplasmic diffusion of chemotaxis components in normal-sized and filamentous E. coli are discussed.Escherichia coli organisms have about six flagella, located randomly around their surfaces, that serve to propel the bacterium. When flagellar rotation is counterclockwise, the flagella form a bundle at one end to push the bacterium forward; this is known as a "run" and typically lasts about 1 to 2 s. When the rotation is clockwise, the flagella pull in opposing directions, causing the bacterium to "tumble" for less than a second. The bacteria alternately run and tumble in the absence of stimuli. When an attractant is encountered, running is promoted and tumbling is suppressed, which causes the bacteria to swim towards the attractant. When a repellent is encountered, the bacteria tumble, which prevents them from swimming into repellent. Adaptation to the attractant or repellent returns the bacteria to unstimulated behavior despite the continued presence of attractant or repellent.Detection of attractants and repellents is mediated by a series of chemoreceptors in the cytoplasmic membrane, the methyl-accepting chemotaxis proteins (MCPs). Binding of repellents induces phosphorylation of the soluble cytoplasmic protein CheY, whereas binding of attractants results in CheY dephosphorylation. CheY interacts with the flagellar motor components and controls the direction of flagellar spin; phosphorylated CheY (CheY-P) stimulates clockwise rotation (tumbling), while unphosphorylated CheY results in counterclockwise rotation (running). For recent reviews of motility and chemotaxis see references 7 and 30.The MCPs are located primarily at t...

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“…The level of CheY-P in vivo is controlled by the autophosphorylation and phosphotransfer activities of the CheA kinase (15,16) and by the dephosphorylation rate of CheY-P. The dephosphorylation rate is controlled by the intrinsic autophosphatase activity of CheY (15,16) and by CheZ activity (15,17).…”

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confidence: 99%