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Port Meadow flooded, February 2021

Professor Richard Berry D. Phil.

Professor of Biological Physics

Research theme

  • Biological physics

Sub department

  • Condensed Matter Physics

Research groups

  • Oxford Molecular Motors
Richard.Berry@physics.ox.ac.uk
Telephone: 01865 (2)72288,01865 (2)71723
Clarendon Laboratory, room 273B
  • About
  • Links
  • Publications

Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging.

Proc Natl Acad Sci U S A 105:40 (2008) 15376-15381

Authors:

Mark C Leake, Nicholas P Greene, Rachel M Godun, Thierry Granjon, Grant Buchanan, Shuyun Chen, Richard M Berry, Tracy Palmer, Ben C Berks

Abstract:

The twin-arginine translocation (Tat) system transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membrane of plant chloroplasts. The essential components of the Tat pathway are the membrane proteins TatA, TatB, and TatC. TatA is thought to form the protein translocating element of the Tat system. Current models for Tat transport make predictions about the oligomeric state of TatA and whether, and how, this state changes during the transport cycle. We determined the oligomeric state of TatA directly at native levels of expression in living cells by photophysical analysis of individual yellow fluorescent protein-labeled TatA complexes. TatA forms complexes exhibiting a broad range of stoichiometries with an average of approximately 25 TatA subunits per complex. Fourier analysis of the stoichiometry distribution suggests the complexes are assembled from tetramer units. Modeling the diffusion behavior of the complexes suggests that TatA protomers associate as a ring and not a bundle. Each cell contains approximately 15 mobile TatA complexes and a pool of approximately 100 TatA molecules in a more disperse state in the membrane. Dissipation of the protonmotive force that drives Tat transport has no affect on TatA complex stoichiometry. TatA complexes do not form in cells lacking TatBC, suggesting that TatBC controls the oligomeric state of TatA. Our data support the TatA polymerization model for the mechanism of Tat transport.
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Characterization and Application of Controllable Local Chemical Changes Produced by Reagent Delivery from a Nanopipet

Journal of the American Chemical Society American Chemical Society (ACS) 130:31 (2008) 10386-10393

Authors:

Joe D Piper, Chao Li, Chien-Jung Lo, Richard Berry, Yuri Korchev, Liming Ying, David Klenerman
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How bacteria change gear

Science 320:5883 (2008) 1599-1600

Authors:

RM Berry, JP Armitage

Abstract:

Bacterial motility is arrested when a protein that acts as a clutch disables rotation of the flagellar motor.
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Microbiology. How bacteria change gear.

Science 320:5883 (2008) 1599-1600

Authors:

Richard M Berry, Judith P Armitage
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Bacterial flagellar motor.

Q Rev Biophys 41:2 (2008) 103-132

Authors:

Yoshiyuki Sowa, Richard M Berry

Abstract:

The bacterial flagellar motor is a reversible rotary nano-machine, about 45 nm in diameter, embedded in the bacterial cell envelope. It is powered by the flux of H+ or Na+ ions across the cytoplasmic membrane driven by an electrochemical gradient, the proton-motive force or the sodium-motive force. Each motor rotates a helical filament at several hundreds of revolutions per second (hertz). In many species, the motor switches direction stochastically, with the switching rates controlled by a network of sensory and signalling proteins. The bacterial flagellar motor was confirmed as a rotary motor in the early 1970s, the first direct observation of the function of a single molecular motor. However, because of the large size and complexity of the motor, much remains to be discovered, in particular, the structural details of the torque-generating mechanism. This review outlines what has been learned about the structure and function of the motor using a combination of genetics, single-molecule and biophysical techniques, with a focus on recent results and single-molecule techniques.
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