Torque-generating units of the flagellar motor of Escherichia coli have a high duty ratio

Article Abstract:

Expression of protein MotA was induced in motA- cells under conditions of low viscous load. The limiting speed of the motor is shown to be independent of the number of units. It is likely that each unit may stay attached to the rotor during its mechanochemical cycle. Torque generators act more like kinesin than myosin.

---

Bacterial flagellar switching under load

Article Abstract:

The authors discuss the study of flagallated bacteria which can modulate rotation direction of their flagellar motors. The probability of the motor rotating in the clockwise direction increases under high load when the motor spins slowly.

United States, Science & research, Physiological aspects, Gene mutations, Gene mutation, Genetic aspects, Biomechanics, Chemotaxis, Sodium channels, Chemical properties

---

Powering the flagellar motor of Escherichia coli with an external voltage source

Article Abstract:

Studies on the effect of proton leakage or mechanical nonlinearities on the efficiency of the rotary motors of the flagella of Escherichia coli show that torque is proportional to protonmotive force until -150 millivolts. Thus a definite number of protons work together to carry the motor through each revolution. When the cells protonmotive force is positive, torque-generating elements, which are most probably the motor proteins MotA and/or MotB, become inactive and can be re-activated by a negative protonmotive force.

Motion

Similar abstracts:

• Abstracts: Molecular evidence regarding the origin of echolocation and flight in bats. Parallel adaptive radiations in tow major clades of placental mammals
• Abstracts: Activated T cells regulate bone loss and joint destruction in adjuvant arthritis through osteoprotegerin ligand
• Abstracts: Activin- and Nodal-related factors control antero-posterior patterning of the zebrafish embryo. The molecular nature of the zebrafish tail organizer
• Abstracts: Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33. Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein

This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.