scholarly journals Twin-Positive Motifs Function as Specific Plastid-Targeting Signals

2020 ◽  
Vol 32 (4) ◽  
pp. 807-807
Author(s):  
Gregory Bertoni
Keyword(s):  
Plastid Targeting ◽  
Targeting Signals

scholarly journals A phylogenetic mosaic plastid proteome and unusual plastid-targeting signals in the green-colored dinoflagellate Lepidodinium chlorophorum

2010 ◽  
Vol 10 (1) ◽  
pp. 191 ◽  
Author(s):  
Marianne A Minge ◽  
Kamran Shalchian-Tabrizi ◽  
Ole K Tørresen ◽  
Kiyotaka Takishita ◽  
Ian Probert ◽  
...  
Keyword(s):  
Plastid Targeting ◽  
Targeting Signals

Transit peptide diversity and divergence: A global analysis of plastid targeting signals

BioEssays ◽  
2007 ◽  
Vol 29 (10) ◽  
pp. 1048-1058 ◽  
Author(s):  
Nicola J. Patron ◽  
Ross F. Waller
Keyword(s):  
Global Analysis ◽  
Transit Peptide ◽  
Plastid Targeting ◽  
Targeting Signals

scholarly journals Protein Import into Hydrogenosomes of Trichomonas vaginalis Involves both N-Terminal and Internal Targeting Signals: a Case Study of Thioredoxin Reductases

2008 ◽  
Vol 7 (10) ◽  
pp. 1750-1757 ◽  
Author(s):  
Marek Mentel ◽  
Verena Zimorski ◽  
Patrick Haferkamp ◽  
William Martin ◽  
Katrin Henze
Keyword(s):  
Trichomonas Vaginalis ◽  
Protein Import ◽  
Atp Synthesis ◽  
Antioxidant Systems ◽  
Low Oxygen ◽  
Oxygen Sensitive ◽  
Targeting Signal ◽  
Targeting Signals ◽  
Thioredoxin Reductases

ABSTRACT The parabasalian flagellate Trichomonas vaginalis harbors mitochondrion-related and H2-producing organelles of anaerobic ATP synthesis, called hydrogenosomes, which harbor oxygen-sensitive enzymes essential to its pyruvate metabolism. In the human urogenital tract, however, T. vaginalis is regularly exposed to low oxygen concentrations and therefore must possess antioxidant systems protecting the organellar environment against the detrimental effects of molecular oxygen and reactive oxygen species. We have identified two closely related hydrogenosomal thioredoxin reductases (TrxRs), the hitherto-missing component of a thioredoxin-linked hydrogenosomal antioxidant system. One of the two hydrogenosomal TrxR isoforms, TrxRh1, carried an N-terminal extension resembling known hydrogenosomal targeting signals. Expression of hemagglutinin-tagged TrxRh1 in transfected T. vaginalis cells revealed that its N-terminal extension was necessary to import the protein into the organelles. The second hydrogenosomal TrxR isoform, TrxRh2, had no N-terminal targeting signal but was nonetheless efficiently targeted to hydrogenosomes. N-terminal presequences from hydrogenosomal proteins with known processing sites, i.e., the alpha subunit of succinyl coenzyme A synthetase (SCSα) and pyruvate:ferredoxin oxidoreductase A, were investigated for their ability to direct mature TrxRh1 to hydrogenosomes. Neither presequence directed TrxRh1 to hydrogenosomes, indicating that neither extension is, by itself, sufficient for hydrogenosomal targeting. Moreover, SCSα lacking its N-terminal extension was efficiently imported into hydrogenosomes, indicating that this extension is not required for import of this major hydrogenosomal protein. The finding that some hydrogenosomal enzymes require N-terminal signals for import but that in others the N-terminal extension is not necessary for targeting indicates the presence of additional targeting signals within the mature subunits of several hydrogenosome-localized proteins.

Mechanism of protein import across the chloroplast envelope

2000 ◽  
Vol 28 (4) ◽  
pp. 485-491 ◽  
Author(s):  
K. Chen ◽  
X. Chen ◽  
D. J. Schnell
Keyword(s):  
Protein Import ◽  
Essential Elements ◽  
Chloroplast Envelope ◽  
Envelope Membrane ◽  
Outer Envelope ◽  
Double Membrane ◽  
Protein Subunits ◽  
Targeting Signals ◽  
Outer Envelope Membrane ◽  
Envelope Membranes

The development and maintenance of chloroplasts relies on the contribution of protein subunits from both plastid and nuclear genomes. Most chloroplast proteins are encoded by nuclear genes and are post-translationally imported into the organelle across the double membrane of the chloroplast envelope. Protein import into the chloroplast consists of two essential elements: the specific recognition of the targeting signals (transit sequences) of cytoplasmic preproteins by receptors at the outer envelope membrane and the subsequent translocation of preproteins simultaneously across the double membrane of the envelope. These processes are mediated via the co-ordinate action of protein translocon complexes in the outer (Toe apparatus) and inner (Tic apparatus) envelope membranes.

scholarly journals Protein Transport into “Complex” Diatom Plastids Utilizes Two Different Targeting Signals

1998 ◽  
Vol 273 (47) ◽  
pp. 30973-30978 ◽  
Author(s):  
Markus Lang ◽  
Kirk E. Apt ◽  
Peter G. Kroth
Keyword(s):  
Protein Transport ◽  
Targeting Signals

Evidence for a novel pathway for the targeting of a Saccharomyces cerevisiae peroxisomal protein belonging to the isomerase/hydratase family

2000 ◽  
Vol 113 (3) ◽  
pp. 533-544
Author(s):  
I.V. Karpichev ◽  
G.M. Small
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Fatty Acids ◽  
Unsaturated Fatty Acids ◽  
Beta Oxidation ◽  
Peroxisomal Protein ◽  
Intracellular Targeting ◽  
Targeting Signals ◽  
Peroxisome Targeting Signals

We, and others, have identified a novel Saccharomyces cerevisiae peroxisomal protein that belongs to the isomerase/hydratase family. The protein, named Dci1p, shares 50% identity with Eci1p, a delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase that acts as an auxiliary enzyme in the beta-oxidation of unsaturated fatty acids. Both of these proteins are localized to peroxisomes, and both contain motifs at their amino- and carboxyl termini that resemble peroxisome targeting signals (PTS) 1 and 2. However, we demonstrate that the putative type 1 signaling motif is not required for the peroxisomal localization of either of these proteins. Furthermore, the correct targeting of Eci1p and Dci1p occurs in the absence of the receptors for the type 1 or type 2 peroxisome targeting pathway. Together, these data suggest a novel mechanism for the intracellular targeting of these peroxisomal proteins.

Protein import into orangelles: Hierarchical targeting signals

Cell ◽  
1986 ◽  
Vol 46 (3) ◽  
pp. 321-322 ◽  
Author(s):  
Alan Colman ◽  
Colin Robinson
Keyword(s):  
Protein Import ◽  
Targeting Signals
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