scholarly journals Transit Peptide Mutations That Impair in Vitro and in Vivo Chloroplast Protein Import Do Not Affect Accumulation of the γ-Subunit of Chloroplast ATPase

1998 ◽  
Vol 116 (3) ◽  
pp. 1179-1190 ◽  
Author(s):  
Karen L. Kindle ◽  
Susan D. Lawrence
Keyword(s):  
Protein Import ◽  
Transit Peptide ◽  
Chloroplast Protein Import ◽  
Chloroplast Protein ◽  
Γ Subunit

scholarly journals Molecular Topology of the Transit Peptide during Chloroplast Protein Import

2018 ◽  
Vol 30 (8) ◽  
pp. 1789-1806 ◽  
Author(s):  
Lynn G.L. Richardson ◽  
Eliana L. Small ◽  
Hitoshi Inoue ◽  
Danny J. Schnell
Keyword(s):  
Protein Import ◽  
Transit Peptide ◽  
Molecular Topology ◽  
Chloroplast Protein Import ◽  
Chloroplast Protein

Analysis of targeting sequences demonstrates that trafficking to the Toxoplasma gondii plastid branches off the secretory system

2000 ◽  
Vol 113 (22) ◽  
pp. 3969-3977 ◽  
Author(s):  
A. DeRocher ◽  
C.B. Hagen ◽  
J.E. Froehlich ◽  
J.E. Feagin ◽  
M. Parsons
Keyword(s):  
Green Fluorescent Protein ◽  
Toxoplasma Gondii ◽  
Protein Import ◽  
Fluorescent Protein ◽  
Signal Sequence ◽  
Transit Peptide ◽  
Green Fluorescent ◽  
Secretory System

Apicomplexan parasites possess a plastid-like organelle called the apicoplast. Most proteins in the Toxoplasma gondii apicoplast are encoded in the nucleus and imported post-translationally. T. gondii apicoplast proteins often have a long N-terminal extension that directs the protein to the apicoplast. It can be modeled as a bipartite targeting sequence that contains a signal sequence and a plastid transit peptide. We identified two nuclearly encoded predicted plastid proteins and made fusions with green fluorescent protein to study protein domains required for apicoplast targeting. The N-terminal 42 amino acids of the apicoplast ribosomal protein S9 directs secretion of green fluorescent protein, indicating that targeting to the apicoplast proceeds through the secretory system. Large sections of the S9 predicted transit sequence can be deleted with no apparent impact on the ability to direct green fluorescent protein to the apicoplast. The predicted transit peptide domain of the S9 targeting sequence directs protein to the mitochondrion in vivo. The transit peptide can also direct import of green fluorescent protein into chloroplasts in vitro. These data substantiate the model that protein targeting to the apicoplast involves two distinct mechanisms: the first involving the secretory system and the second sharing features with typical chloroplast protein import.

scholarly journals In vivo studies on the roles of Tic110, Tic40 and Hsp93 during chloroplast protein import

2004 ◽  
Vol 41 (3) ◽  
pp. 412-428 ◽  
Author(s):  
Sabina Kovacheva ◽  
Jocelyn Bédard ◽  
Ramesh Patel ◽  
Penny Dudley ◽  
David Twell ◽  
...  
Keyword(s):  
Protein Import ◽  
In Vivo Studies ◽  
Chloroplast Protein Import ◽  
Chloroplast Protein

scholarly journals In vivo Studies on the Roles of Tic55-Related Proteins in Chloroplast Protein Import in Arabidopsis thaliana

2009 ◽  
Vol 2 (6) ◽  
pp. 1397-1409 ◽  
Author(s):  
Patrik Boij ◽  
Ramesh Patel ◽  
Christel Garcia ◽  
Paul Jarvis ◽  
Henrik Aronsson
Keyword(s):  
Arabidopsis Thaliana ◽  
Protein Import ◽  
In Vivo Studies ◽  
Chloroplast Protein Import ◽  
Chloroplast Protein ◽  
Related Proteins

In Vitro Analysis of Chloroplast Protein Import

2003 ◽  
Vol 17 (1) ◽  
Author(s):  
Matthew D. Smith ◽  
Danny J. Schnell ◽  
Lynda Fitzpatrick ◽  
Kenneth Keegstra
Keyword(s):  
Protein Import ◽  
Chloroplast Protein Import ◽  
Chloroplast Protein ◽  
Vitro Analysis ◽  
In Vitro Analysis
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