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Items: 1 to 20 of 119


A role for the two-helix finger of the SecA ATPase in protein translocation.

Erlandson KJ, Miller SB, Nam Y, Osborne AR, Zimmer J, Rapoport TA.

Nature. 2008 Oct 16;455(7215):984-7. doi: 10.1038/nature07439.


Mapping polypeptide interactions of the SecA ATPase during translocation.

Bauer BW, Rapoport TA.

Proc Natl Acad Sci U S A. 2009 Dec 8;106(49):20800-5. doi: 10.1073/pnas.0910550106. Epub 2009 Nov 20.


A "push and slide" mechanism allows sequence-insensitive translocation of secretory proteins by the SecA ATPase.

Bauer BW, Shemesh T, Chen Y, Rapoport TA.

Cell. 2014 Jun 5;157(6):1416-29. doi: 10.1016/j.cell.2014.03.063.


Structure of a complex of the ATPase SecA and the protein-translocation channel.

Zimmer J, Nam Y, Rapoport TA.

Nature. 2008 Oct 16;455(7215):936-43. doi: 10.1038/nature07335.


Structural determinants of protein translocation in bacteria: conformational flexibility of SecA IRA1 loop region.

Palladino P, Saviano G, Tancredi T, Benedetti E, Rossi F, Ragone R.

J Pept Sci. 2011 Apr;17(4):263-9. doi: 10.1002/psc.1324. Epub 2011 Feb 18.


Characterization of the supporting role of SecE in protein translocation.

Lycklama a Nijeholt JA, de Keyzer J, Prabudiansyah I, Driessen AJ.

FEBS Lett. 2013 Sep 17;587(18):3083-8. doi: 10.1016/j.febslet.2013.07.046. Epub 2013 Aug 13.


Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking.

Mori H, Ito K.

Proc Natl Acad Sci U S A. 2006 Oct 31;103(44):16159-64. Epub 2006 Oct 23.


Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complex.

Whitehouse S, Gold VA, Robson A, Allen WJ, Sessions RB, Collinson I.

J Cell Biol. 2012 Dec 10;199(6):919-29. doi: 10.1083/jcb.201205191. Epub 2012 Dec 3.


Conformational Changes of the Clamp of the Protein Translocation ATPase SecA.

Chen Y, Bauer BW, Rapoport TA, Gumbart JC.

J Mol Biol. 2015 Jul 17;427(14):2348-59. doi: 10.1016/j.jmb.2015.05.003. Epub 2015 May 14.


Identification of two interaction sites in SecY that are important for the functional interaction with SecA.

van der Sluis EO, Nouwen N, Koch J, de Keyzer J, van der Does C, Tampé R, Driessen AJ.

J Mol Biol. 2006 Sep 1;361(5):839-49. Epub 2006 Jul 15.


Crystal structure of a substrate-engaged SecY protein-translocation channel.

Li L, Park E, Ling J, Ingram J, Ploegh H, Rapoport TA.

Nature. 2016 Mar 17;531(7594):395-399. doi: 10.1038/nature17163. Epub 2016 Mar 7.


SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria.

Huber D, Rajagopalan N, Preissler S, Rocco MA, Merz F, Kramer G, Bukau B.

Mol Cell. 2011 Feb 4;41(3):343-53. doi: 10.1016/j.molcel.2010.12.028.


Cross-linked SecA dimers are not functional in protein translocation.

Or E, Rapoport T.

FEBS Lett. 2007 Jun 12;581(14):2616-20. Epub 2007 May 11.


Bacterial protein translocation requires only one copy of the SecY complex in vivo.

Park E, Rapoport TA.

J Cell Biol. 2012 Sep 3;198(5):881-93. doi: 10.1083/jcb.201205140. Epub 2012 Aug 27.


In vivo cross-linking of the SecA and SecY subunits of the Escherichia coli preprotein translocase.

Manting EH, van der Does C, Driessen AJ.

J Bacteriol. 1997 Sep;179(18):5699-704.


A single amino acid substitution in SecY stabilizes the interaction with SecA.

Manting EH, Kaufmann A, van der Does C, Driessen AJ.

J Biol Chem. 1999 Aug 20;274(34):23868-74.


A dual function for SecA in the assembly of single spanning membrane proteins in Escherichia coli.

Deitermann S, Sprie GS, Koch HG.

J Biol Chem. 2005 Nov 25;280(47):39077-85. Epub 2005 Sep 26.


The bacterial ATPase SecA functions as a monomer in protein translocation.

Or E, Boyd D, Gon S, Beckwith J, Rapoport T.

J Biol Chem. 2005 Mar 11;280(10):9097-105. Epub 2004 Dec 23.


The bacterial SRP receptor, SecA and the ribosome use overlapping binding sites on the SecY translocon.

Kuhn P, Weiche B, Sturm L, Sommer E, Drepper F, Warscheid B, Sourjik V, Koch HG.

Traffic. 2011 May;12(5):563-78. doi: 10.1111/j.1600-0854.2011.01167.x. Epub 2011 Feb 25.

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