scholarly journals The Chloroplast Import Receptor Toc34 Functions as Preprotein-Regulated GTPase

2002 ◽  
Vol 383 (12) ◽  
Author(s):  
M. Jelic ◽  
N. Sveshnikova ◽  
M. Motzkus ◽  
P. Hörth ◽  
J. Soll ◽  
...  
Keyword(s):  
Chloroplast Import ◽  
Import Receptor

scholarly journals The Chloroplast Import Receptor Toc90 Partially Restores the Accumulation of Toc159 Client Proteins in the Arabidopsis thaliana ppi2 Mutant

2011 ◽  
Vol 4 (2) ◽  
pp. 252-263 ◽  
Author(s):  
Sibylle Infanger ◽  
Sylvain Bischof ◽  
Andreas Hiltbrunner ◽  
Birgit Agne ◽  
Sacha Baginsky ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Chloroplast Import ◽  
Client Proteins ◽  
Import Receptor

scholarly journals Modifications at the A-domain of the chloroplast import receptor Toc159

2010 ◽  
Vol 5 (11) ◽  
pp. 1513-1516 ◽  
Author(s):  
Birgit Agne ◽  
Felix Kessler
Keyword(s):  
Chloroplast Import ◽  
Import Receptor

scholarly journals The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64

2006 ◽  
Vol 25 (9) ◽  
pp. 1836-1847 ◽  
Author(s):  
Soumya Qbadou ◽  
Thomas Becker ◽  
Oliver Mirus ◽  
Ivo Tews ◽  
Jürgen Soll ◽  
...  
Keyword(s):  
Molecular Chaperone ◽  
Chloroplast Import ◽  
Precursor Proteins ◽  
Import Receptor

scholarly journals The chloroplast import receptor is an integral membrane protein of chloroplast envelope contact sites.

1990 ◽  
Vol 111 (5) ◽  
pp. 1825-1838 ◽  
Author(s):  
D J Schnell ◽  
G Blobel ◽  
D Pain
Keyword(s):  
Membrane Protein ◽  
Protein Import ◽  
Integral Membrane Protein ◽  
Chloroplast Envelope ◽  
Bisphosphate Carboxylase ◽  
Chloroplast Import ◽  
Chloroplast Membrane ◽  
Phosphate Translocator ◽  
Triton X ◽  
Import Receptor

A chloroplast import receptor from pea, previously identified by antiidiotypic antibodies was purified and its primary structure deduced from its cDNA sequence. The protein is a 36-kD integral membrane protein (p36) with eight potential transmembrane segments. Fab prepared from monospecific anti-p36 IgG inhibits the import of the ribulose-1,5-bisphosphate carboxylase small subunit precursor (pS) by interfering with pS binding at the chloroplast surface. Anti-p36 IgGs are able to immunoprecipitate a Triton X-100 soluble p36-pS complex, suggesting a direct interaction between p36 and pS. This immunoprecipitation was specific as it was abolished by a pS synthetic transit peptide, consistent with the transit sequence receptor function of p36. Immunoelectron microscopy localized p36 to regions of the outer chloroplast membrane that are in close contact with the inner chloroplast membrane. Comparison of the deduced sequence of pea p36 to that of other known proteins indicates a striking homology to a protein from spinach chloroplasts that was previously suggested to be the triose phosphate-3-phosphoglycerate-phosphate translocator (phosphate translocator) (Flügge, U. I., K. Fischer, A. Gross, W. Sebald, F. Lottspeich, and C. Eckerskorn. 1989. EMBO (Eur. Mol. Biol. Organ.) J. 8:39-46). However, incubation of Triton X-100 solubilized chloroplast envelope material with hydroxylapatite indicated that p36 was quantitatively absorbed, whereas previous reports have shown that phosphate translocator activity does not bind to hydroxylapatite (Flügge, U. I., and H. W. Heldt. 1981. Biochim. Biophys. Acta. 638:296-304. These data, in addition to the topology and import inhibition data presented in this report support the assignment of p36 as a receptor for chloroplast protein import, and argue against the assignment of the spinach homologue of this protein as the chloroplast phosphate translocator.

scholarly journals Peroxisome Senescence in Human Fibroblasts

2002 ◽  
Vol 13 (12) ◽  
pp. 4243-4255 ◽  
Author(s):  
Julie E. Legakis ◽  
Jay I. Koepke ◽  
Chris Jedeszko ◽  
Ferdous Barlaskar ◽  
Laura J. Terlecky ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Protein Import ◽  
Human Fibroblasts ◽  
Toxic Metabolite ◽  
Age Related ◽  
Peroxisomal Targeting ◽  
Targeting Signal ◽  
Effects Of Aging ◽  
Antioxidant Enzyme Catalase ◽  
Import Receptor

The molecular mechanisms of peroxisome biogenesis have begun to emerge; in contrast, relatively little is known about how the organelle functions as cells age. In this report, we characterize age-related changes in peroxisomes of human cells. We show that aging compromises peroxisomal targeting signal 1 (PTS1) protein import, affecting in particular the critical antioxidant enzyme catalase. The number and appearance of peroxisomes are altered in these cells, and the organelles accumulate the PTS1-import receptor, Pex5p, on their membranes. Concomitantly, cells produce increasing amounts of the toxic metabolite hydrogen peroxide, and we present evidence that this increased load of reactive oxygen species may further reduce peroxisomal protein import and exacerbate the effects of aging.

scholarly journals Nanoscale distribution of mitochondrial import receptor Tom20 is adjusted to cellular conditions and exhibits an inner-cellular gradient

2011 ◽  
Vol 108 (33) ◽  
pp. 13546-13551 ◽  
Author(s):  
C. A. Wurm ◽  
D. Neumann ◽  
M. A. Lauterbach ◽  
B. Harke ◽  
A. Egner ◽  
...  
Keyword(s):  
Mitochondrial Import ◽  
Import Receptor

scholarly journals Molecular Chaperones Hsp90 and Hsp70 Deliver Preproteins to the Mitochondrial Import Receptor Tom70

Cell ◽  
2003 ◽  
Vol 112 (1) ◽  
pp. 41-50 ◽  
Author(s):  
Jason C. Young ◽  
Nicholas J. Hoogenraad ◽  
F.Ulrich Hartl
Keyword(s):  
Molecular Chaperones ◽  
Mitochondrial Import ◽  
Import Receptor

scholarly journals Structural Basis of Presequence Recognition by the Mitochondrial Protein Import Receptor Tom20

Cell ◽  
2000 ◽  
Vol 100 (5) ◽  
pp. 551-560 ◽  
Author(s):  
Yoshito Abe ◽  
Toshihiro Shodai ◽  
Takanori Muto ◽  
Katsuyoshi Mihara ◽  
Hisayoshi Torii ◽  
...  
Keyword(s):  
Protein Import ◽  
Mitochondrial Protein ◽  
Structural Basis ◽  
Mitochondrial Protein Import ◽  
Import Receptor
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