scholarly journals Identification of peroxisomal targeting signals in cholesterol biosynthetic enzymes: AA-CoA thiolase, HMG-CoA synthase, MPPD, and FPP synthase

2000 ◽  
Vol 41 (12) ◽  
pp. 1921-1935 ◽  
Author(s):  
Lisa M. Olivier ◽  
Werner Kovacs ◽  
Kim Masuda ◽  
Gilbert-Andre Keller ◽  
Skaidrite K. Krisans
Keyword(s):  
Biosynthetic Enzymes ◽  
Peroxisomal Targeting ◽  
Targeting Signals

scholarly journals Identification of Novel Plant Peroxisomal Targeting Signals by a Combination of Machine Learning Methods and in Vivo Subcellular Targeting Analyses

2011 ◽  
Vol 23 (4) ◽  
pp. 1556-1572 ◽  
Author(s):  
Thomas Lingner ◽  
Amr R. Kataya ◽  
Gerardo E. Antonicelli ◽  
Aline Benichou ◽  
Kjersti Nilssen ◽  
...  
Keyword(s):  
Machine Learning ◽  
Subcellular Targeting ◽  
Learning Methods ◽  
Machine Learning Methods ◽  
Peroxisomal Targeting ◽  
Targeting Signals

scholarly journals A Novel FRET Approach Quantifies the Interaction Strength of Peroxisomal Targeting Signals and Their Receptor in Living Cells

Cells ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 2381
Author(s):  
Bernhard Hochreiter ◽  
Cheng-Shoong Chong ◽  
Andreas Hartig ◽  
Sebastian Maurer-Stroh ◽  
Johannes Berger ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Interaction Strength ◽  
Quantitative Measure ◽  
Computational Prediction ◽  
Technical Equipment ◽  
Sequence Element ◽  
Standard Equipment ◽  
Peroxisomal Targeting ◽  
Targeting Signals

Measuring Förster–resonance–energy–transfer (FRET) efficiency allows the investigation of protein–protein interactions (PPI), but extracting quantitative measures of affinity necessitates highly advanced technical equipment or isolated proteins. We demonstrate the validity of a recently suggested novel approach to quantitatively analyze FRET-based experiments in living mammalian cells using standard equipment using the interaction between different type-1 peroxisomal targeting signals (PTS1) and their soluble receptor peroxin 5 (PEX5) as a model system. Large data sets were obtained by flow cytometry coupled FRET measurements of cells expressing PTS1-tagged EGFP together with mCherry fused to the PTS1-binding domain of PEX5, and were subjected to a fitting algorithm extracting a quantitative measure of the interaction strength. This measure correlates with results obtained by in vitro techniques and a two-hybrid assay, but is unaffected by the distance between the fluorophores. Moreover, we introduce a live cell competition assay based on this approach, capable of depicting dose- and affinity-dependent modulation of the PPI. Using this system, we demonstrate the relevance of a sequence element next to the core tripeptide in PTS1 motifs for the interaction strength between PTS1 and PEX5, which is supported by a structure-based computational prediction of the binding energy indicating a direct involvement of this sequence in the interaction.

scholarly journals The unique degradation pathway of the PTS2 receptor, Pex7, is dependent on the PTS receptor/coreceptor, Pex5 and Pex20

2014 ◽  
Vol 25 (17) ◽  
pp. 2634-2643 ◽  
Author(s):  
Danielle Hagstrom ◽  
Changle Ma ◽  
Soumi Guha-Polley ◽  
Suresh Subramani
Keyword(s):  
Matrix Protein ◽  
Protein Import ◽  
Degradation Pathway ◽  
Matrix Proteins ◽  
Receptor Recycling ◽  
Wild Type ◽  
The Matrix ◽  
Peroxisomal Targeting ◽  
Targeting Signals ◽  
The Stability

Peroxisomal matrix protein import uses two peroxisomal targeting signals (PTSs). Most matrix proteins use the PTS1 pathway and its cargo receptor, Pex5. The PTS2 pathway is dependent on another receptor, Pex7, and its coreceptor, Pex20. We found that during the matrix protein import cycle, the stability and dynamics of Pex7 differ from those of Pex5 and Pex20. In Pichia pastoris, unlike Pex5 and Pex20, Pex7 is constitutively degraded in wild-type cells but is stabilized in pex mutants affecting matrix protein import. Degradation of Pex7 is more prevalent in cells grown in methanol, in which the PTS2 pathway is nonessential, in comparison with oleate, suggesting regulation of Pex7 turnover. Pex7 must shuttle into and out of peroxisomes before it is polyubiquitinated and degraded by the proteasome. The shuttling of Pex7, and consequently its degradation, is dependent on the receptor recycling pathways of Pex5 and Pex20 and relies on an interaction between Pex7 and Pex20. We also found that blocking the export of Pex20 from peroxisomes inhibits PTS1-mediated import, suggesting sharing of limited components in the export of PTS receptors/coreceptors. The shuttling and stability of Pex7 are divergent from those of Pex5 and Pex20, exemplifying a novel interdependence of the PTS1 and PTS2 pathways.

scholarly journals Identification of two novel type 1 peroxisomal targeting signals in Arabidopsis thaliana

2014 ◽  
Vol 116 (8) ◽  
pp. 1307-1312 ◽  
Author(s):  
Rigoberto A. Ramirez ◽  
Brian Espinoza ◽  
Ernest Y. Kwok
Keyword(s):  
Arabidopsis Thaliana ◽  
Peroxisomal Targeting ◽  
Targeting Signals

Peroxisomal targeting signals in green algae

PROTOPLASMA ◽  
2009 ◽  
Vol 235 (1-4) ◽  
pp. 57-66 ◽  
Author(s):  
Akiko Shinozaki ◽  
Nagisa Sato ◽  
Yasuko Hayashi
Keyword(s):  
Green Algae ◽  
Peroxisomal Targeting ◽  
Targeting Signals

scholarly journals Multiple Distinct Targeting Signals in Integral Peroxisomal Membrane Proteins

2001 ◽  
Vol 153 (6) ◽  
pp. 1141-1150 ◽  
Author(s):  
Jacob M. Jones ◽  
James C. Morrell ◽  
Stephen J. Gould
Keyword(s):  
Membrane Proteins ◽  
Matrix Proteins ◽  
Membrane Biogenesis ◽  
Peroxisomal Membrane ◽  
Interesting Possibility ◽  
Peroxisomal Targeting ◽  
Targeting Signal ◽  
Targeting Signals ◽  
Peroxisome Membrane ◽  
Metabolite Transporter

Peroxisomal proteins are synthesized on free polysomes and then transported from the cytoplasm to peroxisomes. This process is mediated by two short well-defined targeting signals in peroxisomal matrix proteins, but a well-defined targeting signal has not yet been described for peroxisomal membrane proteins (PMPs). One assumption in virtually all prior studies of PMP targeting is that a given protein contains one, and only one, distinct targeting signal. Here, we show that the metabolite transporter PMP34, an integral PMP, contains at least two nonoverlapping sets of targeting information, either of which is sufficient for insertion into the peroxisome membrane. We also show that another integral PMP, the peroxin PEX13, also contains two independent sets of peroxisomal targeting information. These results challenge a major assumption of most PMP targeting studies. In addition, we demonstrate that PEX19, a factor required for peroxisomal membrane biogenesis, interacts with the two minimal targeting regions of PMP34. Together, these results raise the interesting possibility that PMP import may require novel mechanisms to ensure the solubility of integral PMPs before their insertion in the peroxisome membrane, and that PEX19 may play a central role in this process.

scholarly journals Functional characterization of peroxisome biogenic proteins Pex5 and Pex7 of Drosophila

2018 ◽  
Author(s):  
Francesca Di Cara ◽  
Richard A. Rachubinski ◽  
Andrew J. Simmonds
Keyword(s):  
Human Fibroblasts ◽  
Functional Characterization ◽  
Early Death ◽  
Peroxisome Biogenesis ◽  
Developmental Defects ◽  
Peroxisomal Targeting ◽  
Embryonic Nervous System ◽  
Bona Fide ◽  
Targeting Signals

ABSTRACTPeroxisomes are ubiquitous membrane-enclosed organelles involved in lipid processing and reactive oxygen detoxification. Mutations in human peroxisome biogenesis genes (Peroxin, PEX) cause progressive developmental disabilities and, in severe cases, early death. PEX5 and PEX7 are receptors that recognize different peroxisomal targeting signals called PTS1 and PTS2, respectively, and traffic proteins to the peroxisomal matrix. We characterized mutants of Drosophila melanogaster Pex5 and Pex7 and found that adult animals are affected in lipid processing. Moreover, Pex5 mutants exhibited severe developmental defects in the embryonic nervous system and muscle, similar to what is observed in humans with Pex5 mutations, while Pex7 fly mutants were weakly affected in brain development, suggesting different roles for Pex7 in fly and human. Of note, although no PTS2-containing protein has been identified in Drosophila, Pex7 from Drosophila can function as a bona fide PTS2 receptor because it can rescue targeting of the PTS2-containing protein Thiolase to peroxisomes in PEX7 mutant human fibroblasts.

Structures of Type 2 Peroxisomal Targeting Signals in Two Trypanosomatid Aldolases

2000 ◽  
Vol 300 (4) ◽  
pp. 697-707 ◽  
Author(s):  
David M. Chudzik ◽  
Paul A. Michels ◽  
Stéphane de Walque ◽  
Wim G.J. Hol
Keyword(s):  
Peroxisomal Targeting ◽  
Targeting Signals
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