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Requirements for a conservative protein translocation pathway in chloroplasts
Author(s) -
Vojta Lea,
Soll Jürgen,
Bölter Bettina
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.05.004
Subject(s) - protein subunit , chromosomal translocation , chloroplast , chaperone (clinical) , translocon , thylakoid , microbiology and biotechnology , chemistry , atp hydrolysis , twin arginine translocation pathway , biochemistry , biophysics , biology , atpase , enzyme , gene , medicine , pathology
The chloroplast inner envelope translocon subunit Tic110 is imported via a soluble stromal translocation intermediate. In this study an in‐organellar import system is established which allows for an accumulation of this intermediate in order to analyze its requirements for reexport. All results demonstrate that the re‐export of Tic110 from the soluble intermediate stage into the inner envelope requires ATP hydrolysis, which cannot be replaced by other NTPs. Furthermore, the molecular chaperone Hsp93 seems prominently involved in the reexport pathway of Tic110, because other stromal intermediates like that of the oxygen evolving complex subunit OE33 (iOE33) en route to the thylakoid lumen interacts preferentially with Hsp70.