The motor protein prestin is a bullet-shaped molecule with inner cavities

  • Mio K
  • Kubo Y
  • Ogura T
 et al. 
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Abstract

Prestin is a transmembrane motor protein localized at the outer hair
cells (OHCs) of the mammalian inner ear. Voltage-dependent conformational
changes in prestin generate changes in the length of OHCs. A loss
of prestin function is reported to induce severe auditory deficiencies,
suggesting prestin-dependent changes of OHC length may be at least
a part of cochlear amplification. Here we expressed the recombinant
FLAG-fused prestin proteins in Sf9 cells and purified to particles
of a uniform size in EM. The square-shaped top view of purified prestin,
the binding of multiple anti-FLAG antibodies to each prestin particle,
the native-PAGE analysis, and the much larger molecular weight obtained
from size exclusion chromatography than the estimation for the monomer
all support that prestin is a tetramer (Zheng, J., Du, G. G., Anderson,
C. T., Keller, J. P., Orem, A., Dallos, P., and Cheatham, M. (2006)
J. Biol. Chem. 281, 19916-19924). From negatively stained prestin
particles, the three-dimensional structure was reconstructed at 2
nm resolution assuming 4-fold symmetry. Prestin is shown to be a
bullet-shaped particle with a large cytoplasmic domain. The surface
representation demonstrates indentations on the molecule, and the
slice images indicate the inner cavities of sparse densities. The
dimensions, 77 � 77 � 115�, are consistent with the previously reported
sizes of motor proteins on the surface of OHCs.

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