Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on March 3, 2006
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
281/9/5476    most recent
M512453200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dabney-Smith, C.
Right arrow Articles by Cline, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dabney-Smith, C.
Right arrow Articles by Cline, K.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print December 30, 2005
J. Biol. Chem, 10.1074/jbc.M512453200
Submitted on November 21, 2005
Revised on December 30, 2005
Accepted on December 30, 2005

Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport

Carole Dabney-Smith, Hiroki Mori, and Kenneth Cline

Horticultural Sciences, University of Florida, Gainesville, FL 32611

Corresponding Author: kcline{at}ufl.edu

The twin arginine translocation (Tat) systems of thylakoids and bacteria transport fully folded protein substrates without breaching the permeability barrier of the membrane. Two components of the thylakoid system, cpTatC and Hcf106, comprise a precursor receptor complex. The third component, Tha4, assembles with the precursor receptor complex for the translocation step and is thought to comprise at least part of the protein-conducting channel. Here we used two different cross-linking approaches to explore the organization of Tha4 in the translocase. These cross-linking techniques showed that transition to an active protein transport state results in an alignment of Tha4 amphipathic helix and carboxyl tail domains to form Tha4 oligomers. Oligomer-ization required functional Tha4, a twin arginine signal peptide, and an active cpTatC-Hcf106 receptor complex. The spectrum of oligomers obtained was independent of the mature folded domain of the precursor. We propose a trapdoor mechanism for trans-location whereby aligned oligomers of Tha4 amphipathic helices fold into the membrane to allow form-fitting passage of precursor proteins.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
S. Panahandeh, C. Maurer, M. Moser, M. P. DeLisa, and M. Muller
Following the Path of a Twin-arginine Precursor along the TatABC Translocase of Escherichia coli
J. Biol. Chem., November 28, 2008; 283(48): 33267 - 33275.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M. C. Leake, N. P. Greene, R. M. Godun, T. Granjon, G. Buchanan, S. Chen, R. M. Berry, T. Palmer, and B. C. Berks
Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging
PNAS, October 7, 2008; 105(40): 15376 - 15381.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
F. Berthelmann, D. Mehner, S. Richter, U. Lindenstrauss, H. Lunsdorf, G. Hause, and T. Bruser
Recombinant Expression of tatABC and tatAC Results in the Formation of Interacting Cytoplasmic TatA Tubes in Escherichia coli
J. Biol. Chem., September 12, 2008; 283(37): 25281 - 25289.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. M. L. Barrett, R. Freudl, and C. Robinson
Twin Arginine Translocation (Tat)-dependent Export in the Apparent Absence of TatABC or TatA Complexes Using Modified Escherichia coli TatA Subunits That Substitute for TatB
J. Biol. Chem., December 14, 2007; 282(50): 36206 - 36213.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Richter, U. Lindenstrauss, C. Lucke, R. Bayliss, and T. Bruser
Functional Tat Transport of Unstructured, Small, Hydrophilic Proteins
J. Biol. Chem., November 16, 2007; 282(46): 33257 - 33264.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. B. Gould, E. Fan, F. Hempel, U.-G. Maier, and R. B. Klosgen
Translocation of a Phycoerythrin {alpha} Subunit across Five Biological Membranes
J. Biol. Chem., October 12, 2007; 282(41): 30295 - 30302.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. P. Greene, I. Porcelli, G. Buchanan, M. G. Hicks, S. M. Schermann, T. Palmer, and B. C. Berks
Cysteine Scanning Mutagenesis and Disulfide Mapping Studies of the TatA Component of the Bacterial Twin Arginine Translocase
J. Biol. Chem., August 17, 2007; 282(33): 23937 - 23945.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
F. Sargent
Constructing the wonders of the bacterial world: biosynthesis of complex enzymes
Microbiology, March 1, 2007; 153(3): 633 - 651.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
F. Gerard and K. Cline
The Thylakoid Proton Gradient Promotes an Advanced Stage of Signal Peptide Binding Deep within the Tat Pathway Receptor Complex
J. Biol. Chem., February 23, 2007; 282(8): 5263 - 5272.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
Y. Kikuchi, M. Date, H. Itaya, K. Matsui, and L.-F. Wu
Functional Analysis of the Twin-Arginine Translocation Pathway in Corynebacterium glutamicum ATCC 13869
Appl. Envir. Microbiol., November 1, 2006; 72(11): 7183 - 7192.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement