Peroxisome protein import: some answers, more questions

Baker, Alison; Sparkes, Imogen

doi:10.1016/j.pbi.2005.09.009

Cited by 53 publications

(28 citation statements)

References 58 publications

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“…After translocation, PEX7 is recycled back to the cytoplasm (Baker and Sparkes, 2005). It is tempting to speculate that the lack of PTS2 processing in deg15 plants might interfere with the successful relocation of PTS2 recognition factor PEX7 to the cytoplasm because the machinery involved in this process is not yet well understood (Baker and Sparkes, 2005).…”

Section: Resultsmentioning

confidence: 99%

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The DEG15 Serine Protease Cleaves Peroxisomal Targeting Signal 2-Containing Proteins in Arabidopsis

et al. 2008

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Two distinct peroxisomal targeting signals (PTSs), the C-terminal PTS1 and the N-terminal PTS2, are defined. Processing of the PTS2 on protein import is conserved in higher eukaryotes. Recently, candidates for the responsible processing protease were identified from plants (DEG15) and mammals (TYSND1). We demonstrate that plants lacking DEG15 show an expressed phenotype potentially linked to reduced b-oxidation, indicating the impact of protein processing on peroxisomal functions in higher eukaryotes. Mutational analysis of Arabidopsis (Arabidopsis thaliana) DEG15 revealed that conserved histidine, aspartic acid, and serine residues are essential for the proteolytic activity of this enzyme in vitro. This indicates that DEG15 and related enzymes are trypsin-like serine endopeptidases. Deletion of a plant-specific stretch present in the protease domain diminished, but did not abolish, the proteolytic activity of DEG15 against the PTS2-containing glyoxysomal malate dehydrogenase. Fluorescence microscopy showed that a DEG15-green fluorescent protein fusion construct is targeted to peroxisomes in planta. In vivo studies with isolated homozygous deg15 knockout mutants and complemented mutant lines suggest that this enzyme mediates general processing of PTS2-containing proteins.

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Section: Resultsmentioning

confidence: 99%

“…All peroxisomal proteins are encoded in the nucleus, synthesized on cytosolic ribosomes, and imported as folded proteins with one of two peroxisomal targeting signals (PTSs; Baker and Sparkes, 2005). PTS1 is a C-terminal tripeptide with the consensus sequence SerLys-Leu (SKL; Swinkels et al, 1991).…”

mentioning

confidence: 99%

The DEG15 Serine Protease Cleaves Peroxisomal Targeting Signal 2-Containing Proteins in Arabidopsis

et al. 2008

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“…However, cleavage of C-terminal signals is biologically relevant as illustrated by peroxisomal proteins which carry their localization sequence at the C-terminus. 48 To assess the origin of the unpredicted protein C-termini, we determined the occurrence of each amino acid at the two final positions of the identified 361 identified protein C-termini. The full sequences of all identified C-terminal peptides are given in Supporting Information Table 3C,D.…”

Section: Identification Of Protein Termini Regardless Of Theirmentioning

confidence: 99%

Targeted Analysis of Protein Termini

et al. 2007

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We describe a targeted analysis of protein isoforms by selective enrichment and identification of in vivo acetylated protein N-termini and protein C-termini. Our method allows the characterization of these protein termini regardless of their annotation in protein databases and requires no chemical derivatization. Using an iterative database search strategy that takes account of the enrichment protocol, 263 IPI annotated and 87 unpredicted acetylated N-termini were identified in the crude membrane fraction of human embryonic carcinoma cells. The N-acetylated peptides conform to the reported criteria for in vivo modification. In addition, 168 IPI annotated and 193 unpredicted C-termini were identified. Additionally, and for the first time, we also report on in vivo N-terminal propionylation. The significant number of unknown protein N-and C-termini suggests a high degree of novel transcription independent of annotated gene boundaries and/or specific protein processing. Biological relevance of several of these unpredicted protein termini could be curated from the literature, adding further weight to the argument to go beyond routine database search strategies. Our method will improve the correct annotation of genes and proteins in databases.

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“…In addition, these organelles contain an import machinery capable of importing completely folded proteins [76][77][78][79] , and have a controlled way of proliferation [80][81][82] . So, peroxisomes have the same origin as secretory vesicles and are thus candidates for alternative trafficking of proteins.…”

Section: Engineering Membrane Trafficking As a Novel Conceptmentioning

confidence: 99%

Peroxicretion, a Novel Tool for Engineering Membrane Trafficking

Sagt¹

2012

Crosstalk and Integration of Membrane Trafficking Pathways

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Peroxisome protein import: some answers, more questions

Cited by 53 publications

References 58 publications

The DEG15 Serine Protease Cleaves Peroxisomal Targeting Signal 2-Containing Proteins in Arabidopsis

The DEG15 Serine Protease Cleaves Peroxisomal Targeting Signal 2-Containing Proteins in Arabidopsis

Targeted Analysis of Protein Termini

Peroxicretion, a Novel Tool for Engineering Membrane Trafficking

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