help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH

Biophys. J. BioFAST: First Published May 18, 2007. doi:10.1529/biophysj.106.098731
© 2007 by the Biophysical Society.


A more recent version of this article appeared on September 15, 2007.
This Article
Right arrow Full Text (Rapid PDF)
Right arrow All Versions of this Article:
biophysj.106.098731v1
93/6/1993    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 arrow Author home page(s):
Steven Theg
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Braun, N. A
Right arrow Articles by Theg, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Braun, N. A
Right arrow Articles by Theg, S.

MEMBRANES

The chloroplast Tat pathway utilizes the transmembrane electric potential as an energy source

Nikolai A Braun 1, Andrew W Davis 1 and Steven Theg 1*

1 University of California - Davis

* To whom correspondence should be addressed. E-mail: smtheg{at}ucdavis.edu.

Submitted on October 3, 2006
Revised on November 14, 2006
Accepted on 2 May 2007


   Abstract
The thylakoid membrane, located inside the chloroplast, requires proteins transported across it for plastid biogenesis and functional photosynthetic electron transport. The chloroplast Tat translocator found on thylakoids transports proteins from the plastid stroma to the thylakoid lumen. Previous studies have shown that the chloroplast Tat pathway is independent of NTP hydrolysis as an energy source and instead depends on the thylakoid transmembrane proton gradient to power protein translocation. Due to it's localization on the same membrane as the proton motive force dependent F0F1 ATPase, we believed that the chloroplast Tat pathway also made use of the thylakoid electric potential for transporting substrates. By adjusting the rate of photosynthetic proton pumping and by utilizing ionophores, we show that the chloroplast Tat pathway can also utilize the transmembrane electric potential for protein transport. Our findings indicate that the chloroplast Tat pathway is likely dependent on the total protonmotive force (PMF) as an energy source. As a PMF-dependent device, certain predictions can be made about structural features expected to be found in the Tat translocon; specifically, the presence of a proton well, a device in the membrane that converts electrical potential into chemical potential.

Key Words: Tat pathway, protein transport, protonmotive force, thylakoid, twin arginine




This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
N. A. Braun and S. M. Theg
The Chloroplast Tat Pathway Transports Substrates in the Dark
J. Biol. Chem., April 4, 2008; 283(14): 8822 - 8828.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2007 by the Biophysical Society.