Arsenate arrests flagellar rotation in cytoplasm-free envelopes of bacteria.
The effect of arsenate on flagellar rotation in cytoplasm-free flagellated envelopes of Escherichia coli and Salmonella typhimurium was investigated. Flagellar rotation ceased as soon as the envelopes were exposed to arsenate. Inclusion of phosphate intracellularly (but not extracellular) prevented the inhibition by arsenate. In a parallel experiment, the rotation was not affected by inclusion of an ATP trap (hexokinase and glucose) within the envelopes. It is concluded that arsenate affects the motor in a way other than reversible deenergization. This may be an irreversible damage to the cell or direct inhibition of the motor by arsenate. The latter possibility suggests that a process of phosphorylation or phosphate binding is involved in the motor function.
Margolin
Y
Y
Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot, Israel.
Barak
R
R
Eisenbach
M
M
D000255:Adenosine Triphosphate / Q000378:metabolism; D001149:Arsenates / Q000494:pharmacology*; D002462:Cell Membrane / Q000187:drug effects / Q000502:physiology; D002465:Cell Movement / Q000187:drug effects; D003593:Cytoplasm / Q000502:physiology; D004579:Electron Transport / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects / Q000502:physiology*; D005407:Flagella / Q000187:drug effects / Q000502:physiology*; D010766:Phosphorylation; D012486:Salmonella typhimurium / Q000187:drug effects / Q000502:physiology*
D001149:Arsenates; D000255:Adenosine Triphosphate; C025657:arsenic acid