One SecY is enough

نویسنده

  • Nicole LeBrasseur
چکیده

Lattice supports single bilayer he spherical membrane surrounding the poxvirus genome begins to form as an open, cup-like structure. Some have argued that the edge of the cup must be composed of two closely apposed membranes (imagine a collapsed vesicle); otherwise, the hydrophobic edges of a single membrane would be exposed to the cytoplasm. But on page 269, John Heuser confirms that poxvirus has only a single membrane bilayer. He finds that the growing membrane is stabilized by a proteinaceous lattice. Heuser imaged freeze-fractured cells infected with poxvirus. Freeze-fracturing T

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Protein Translocation Is Mediated by Oligomers of the SecY Complex with One SecY Copy Forming the Channel

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The transport of proteins across the plasma membrane in bacteria requires a channel formed from the SecY complex, which cooperates with either a translating ribosome in cotranslational translocation or the SecA ATPase in post-translational translocation. Whether translocation requires oligomers of the SecY complex is an important but controversial issue: it determines channel size, how the perm...

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Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane

In prokaryotes, about one third of cellular proteins are translocated across the plasma membrane or inserted into it by concerted action of the cytoplasmic ATPase SecA and the universally conserved SecYEG heterotrimeric polypeptide-translocating pore. Secretion complexes have been reported to localize in specific subcellular sites in Bacillus subtilis. In this work, we used a combination of tot...

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Mapping polypeptide interactions of the SecA ATPase during translocation.

Many bacterial proteins, including most secretory proteins, are translocated across the plasma membrane by the interplay of the cytoplasmic SecA ATPase and a protein-conducting channel formed by the SecY complex. SecA catalyzes the sequential movement of polypeptide segments through the SecY channel. How SecA interacts with a broad range of polypeptide segments is unclear, but structural data r...

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SecY, a component of the protein translocation system in Escherichia coli, was depleted at a nonpermissive temperature in a strain which had a temperature-sensitive polar effect on the expression of its secY. Membrane vesicles prepared from these cells, when grown at the nonpermissive temperature, contained about 5% SecY and similarly low levels of SecG. As expected, translocation of alkaline p...

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عنوان ژورنال:
  • The Journal of Cell Biology

دوره 169  شماره 

صفحات  -

تاریخ انتشار 2005