Measurement of the Energetics of Protein Transport Across the Chloroplast Thylakoid Membrane

Author(s):  
Steven M. Theg
FEBS Journal ◽  
2009 ◽  
Vol 276 (5) ◽  
pp. 1177-1186 ◽  
Author(s):  
Cassie Aldridge ◽  
Peter Cain ◽  
Colin Robinson

2008 ◽  
Vol 283 (49) ◽  
pp. 33838-33845 ◽  
Author(s):  
Stefan Frielingsdorf ◽  
Mario Jakob ◽  
Ralf Bernd Klösgen

1991 ◽  
pp. 605-610
Author(s):  
Colin Robinson ◽  
Ruth Mould ◽  
Jamie Shackleton

Author(s):  
Ruth M. Mould ◽  
Julie W. Meadows ◽  
Jamie B. Shackleton ◽  
Colin Robinson

1994 ◽  
Vol 126 (2) ◽  
pp. 365-374 ◽  
Author(s):  
T A Smith ◽  
B D Kohorn

The apparatus that permits protein translocation across the internal thylakoid membranes of chloroplasts is completely unknown, even though these membranes have been the subject of extensive biochemical analysis. We have used a genetic approach to characterize the translocation of Chlamydomonas cytochrome f, a chloroplast-encoded protein that spans the thylakoid once. Mutations in the hydrophobic core of the cytochrome f signal sequence inhibit the accumulation of cytochrome f, lead to an accumulation of precursor, and impair the ability of Chlamydomonas cells to grow photosynthetically. One hydrophobic core mutant also reduces the accumulation of other thylakoid membrane proteins, but not those that translocate completely across the membrane. These results suggest that the signal sequence of cytochrome f is required and is involved in one of multiple insertion pathways. Suppressors of two signal peptide mutations describe at least two nuclear genes whose products likely describe the translocation apparatus, and selected second-site chloroplast suppressors further define regions of the cytochrome f signal peptide.


1993 ◽  
Vol 12 (11) ◽  
pp. 4105-4114 ◽  
Author(s):  
K. Cline ◽  
R. Henry ◽  
C. Li ◽  
J. Yuan

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