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  The Bacterial Protein-Translocation Complex: SecYEG Dimers Associate with One or Two SecA Molecules

Tziatzios, C., Schubert, D., Lotz, M., Gundogan, D., Betz, H., Schägger, H., et al. (2004). The Bacterial Protein-Translocation Complex: SecYEG Dimers Associate with One or Two SecA Molecules. Journal of Molecular Biology, 340(3), 513-524. doi:10.1016/j.jmb.2004.04.076.

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Tziatzios, Christos1, Author
Schubert, Dieter1, Author
Lotz, Mirko2, Author           
Gundogan, Derya1, Author
Betz, Heidi2, Author           
Schägger, Hermann1, Author
Haase, Winfried2, 3, Author           
Duong, Franck1, Author
Collinson, Ian2, Author           
Affiliations:
1External Organizations, ou_persistent22              
2Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
3Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068297              

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 Abstract: In bacteria, the Sec-protein transport complex facilitates the passage of most secretory and membrane proteins across and into the plasma membrane. The core complex SecYEG forms the protein channel and engages either ribosomes or the ATPase SecA, which drive translocation of unfolded polypeptide chains through the complex and into the periplasmic space. Escherichia coli SecYEG forms dimers in membranes, but in detergent solution the population of these dimers is low. However, we find that stable dimers can be assembled by the addition of a monoclonal antibody. Normally, a stable SecYEG-SecA complex can only form on isolated membranes or on reconstituted proteo-liposomes. The antibody-stabilised SecYEG dimer binds one SecA molecule in detergent solution. In the presence of AMPPNP, a non-hydrolysable analogue of ATP, a complex forms containing one antibody and two each of SecYEG and SecA. SecYEG monomers or tetramers do not associate to a significant degree with SecA. The observed variability in the stoichiometry of SecYEG and SecA association and its nucleotide modulation may be important and necessary for the protein translocation reaction.

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Language(s): eng - English
 Dates: 2004
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 227054
DOI: 10.1016/j.jmb.2004.04.076
 Degree: -

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Title: Journal of Molecular Biology
  Other : JMB
  Abbreviation : J. Mol. Biol.
Source Genre: Journal
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Publ. Info: Elsevier
Pages: - Volume / Issue: 340 (3) Sequence Number: - Start / End Page: 513 - 524 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/0022-2836