The bacterial ATPase SecA functions as a monomer in protein translocation

The ATPase SecA drives the post-translational translocation of proteins through the SecY channel in the bacterial inner membrane. SecA is a dimer that can dissociate into monomers under certain conditions. To address the functional importance of the monomeric state, we generated an Escherichia coli...

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Vydáno v:	The Journal of biological chemistry Ročník 280; číslo 10; s. 9097
Hlavní autoři:	Or, Eran, Boyd, Dana, Gon, Stéphanie, Beckwith, Jonathan, Rapoport, Tom
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States 11.03.2005
Témata:	Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Amino Acid Sequence Bacillus subtilis - enzymology Bacillus subtilis - growth & development Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Escherichia coli - enzymology Kinetics Membrane Transport Proteins - chemistry Membrane Transport Proteins - genetics Membrane Transport Proteins - metabolism Models, Molecular Plasmids - genetics Protein Structure, Secondary Protein Subunits - chemistry Proteolipids - metabolism Recombinant Proteins - chemistry Recombinant Proteins - metabolism SEC Translocation Channels SecA Proteins Sequence Deletion
ISSN:	0021-9258
On-line přístup:	Zjistit podrobnosti o přístupu
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