Oligomeric states of the SecA and SecYEG core components of the bacterial Sec translocon

Many proteins synthesized in the cytoplasm ultimately function in non-cytoplasmic locations. In Escherichia coli, the general secretory (Sec) pathway transports the vast majority of these proteins. Two fundamental components of the Sec transport pathway are the SecYEG heterotrimeric complex that for...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2007-01, Vol.1768 (1), p.5-12
Main Authors: Rusch, Sharyn L., Kendall, Debra A.
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - metabolism
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Dimerization
Escherichia coli - metabolism
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - metabolism
Membrane Proteins - chemistry
Membrane Transport Proteins - chemistry
Membrane Transport Proteins - metabolism
Models, Molecular
Molecular Motor Proteins - chemistry
Molecular Motor Proteins - metabolism
Oligomer
Protein Conformation
Protein Transport
SEC Translocation Channels
SecA
SecYEG
Translocon
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Summary:Many proteins synthesized in the cytoplasm ultimately function in non-cytoplasmic locations. In Escherichia coli, the general secretory (Sec) pathway transports the vast majority of these proteins. Two fundamental components of the Sec transport pathway are the SecYEG heterotrimeric complex that forms the channel through the cytoplasmic membrane, and SecA, the ATPase that drives the preprotein to and across the membrane. This review focuses on what is known about the oligomeric states of these core Sec components and how the oligomeric state might change during the course of the translocation of a preprotein.
ISSN:0005-2736
0006-3002
1879-2642
DOI:10.1016/j.bbamem.2006.08.013