Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138.
Published: June 2019
AI Article Synopsis
Article Abstract
Multisubunit protein complexes are ubiquitous in biology and perform a plethora of essential functions. Most of the scientific literature treats such assemblies as static: their function is assumed to be independent of their manner of assembly, and their structure is assumed to remain intact until they are degraded. Recent observations of the bacterial flagellar motor, among others, bring these notions into question. The torque-generating stator units of the motor assemble and disassemble in response to changes in load. Here, we used electrorotation to drive tethered cells forward, which decreases motor load, and measured the resulting stator dynamics. No disassembly occurred while the torque remained high, but all of the stator units were released when the motor was spun near the zero-torque speed. When the electrorotation was turned off, so that the load was again high, stator units were recruited, increasing motor speed in a stepwise fashion. A model in which speed affects the binding rate and torque affects the free energy of bound stator units captures the observed torque-dependent stator assembly dynamics, providing a quantitative framework for the environmentally regulated self-assembly of a major macromolecular machine.
The bacterial flagellar motor (BFM) is a rotary molecular machine that drives critical bacterial processes including motility, chemotaxis, biofilm formation, and infection. For over two decades, the bead assay, which measures the rotation of a microparticle attached to the flagellum of a surface-attached bacterium, has been instrumental in deciphering the motor's biophysical mechanisms. This technique has not only quantified the rotational speed and frequency of directional switching as a function of the viscous load on the flagellum but has also revealed the BFM's capacity for mechanosensitive speed modulation, adapting to environmental conditions.
This study aims to optimize the reduction of free fatty acids (FFAs) in palm fatty acid distillate (PFAD) using hydrodynamic cavitation reactors (HCRs) in series and a solid acid catalyst for biodiesel production. Hydrodynamic cavitation is used to accelerate the esterification of FFAs using a heterogeneous acid catalyst. There are three HCRs units, and each HCR composed of a 3D-printed rotor and stator, is separated by flanges and equipped with a basket for holding Amberlyst-15 catalyst.
MotY homologs are present in a variety of monotrichous bacterial strains and are thought to form an additional structural T ring in flagellar motors. While MotY potentially plays an important role in motor torque generation, its impact on motor output dynamics remains poorly understood. In this study, we investigate the role of MotY in P.
Many bacteria use the type 9 secretion system (T9SS) for both moving smoothly (gliding motility) and for secreting proteins.
The T9SS acts like a rotating motor powered by proton motive force, acting as a "molecular snowmobile" to facilitate movement along the bacterial membrane.
A recent discovery shows that altering a specific part of the conveyor belt protein can switch the rotation of T9SS from counterclockwise to clockwise, revealing a mechanism that allows the conveyor belt to influence the motion and direction of the T9SS.
