Redox-regulated Cargo Binding and Release by the Peroxisomal Targeting Signal Receptor, Pex5

Ma, Changle; Hagstrom, Danielle; Polley, Soumi Guha; Subramani, Suresh

doi:10.1074/jbc.m113.492694

Cited by 71 publications

(60 citation statements)

References 39 publications

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“…These results contrast previous reports indicating that LdPEX5 tended to form a tetramer [33]. This difference in quaternary structure is likely due to disulfide bond formation as previously documented [38]. A similar analysis of ldpex14 showed that this fragment eluted as ~35 kDa species, a size corresponding to a homodimer [25].…”

Section: Quaternary Structure Of Ldpex5-ldpex14 Complexescontrasting

confidence: 99%

The Leishmania donovani peroxin 14 binding domain accommodates a high degeneracy in the pentapeptide motifs present on peroxin 5

Hojjat

Jardim

2015

Biochimica et Biophysica Acta (BBA) - General Subjects

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Section: Quaternary Structure Of Ldpex5-ldpex14 Complexescontrasting

confidence: 99%

The Leishmania donovani peroxin 14 binding domain accommodates a high degeneracy in the pentapeptide motifs present on peroxin 5

Hojjat

Jardim

2015

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…36 One surprising observation is that the binding affinity of all the peptides tested in the present study was, within experimental error, identical for both truncated and full length PEX5. Since the N terminally truncated PEX5C lacks this redox sensitive Cys such a mechanism would appear not to be relevant in the context of the binding of short peptides in our experimental system.…”

Section: Implications For Cargo Binding To Pex5mentioning

confidence: 55%

Experimental Validation of Plant Peroxisomal Targeting Prediction Algorithms by Systematic Comparison of In Vivo Import Efficiency and In Vitro PTS1 Binding Affinity

Skoulding

Chowdhary

Deus

et al. 2015

Journal of Molecular Biology

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Most peroxisomal matrix proteins possess a C-terminal targeting signal type 1 (PTS1).Accurate prediction of functional PTS1 sequences and their relative strength by computational methods is essential for determination of peroxisomal proteomes in silico, but has proved challenging, due to high sequence variability of non-canonical targeting signals, particularly in higher plants, and low availability of experimentally validated non-canonical examples. In this study in silico predictions were compared with in vivo targeting analyses 2 and in vitro thermodynamic binding of mutated variants within the context of one model targeting sequence. There was broad agreement between the methods for entire PTS1 domains and position-specific single amino acid (aa) residues, including residues upstream of the PTS1 tripeptide. The hierarchy Leu>Met>Ile>Val at the C-terminal position was determined for all methods but both experimental approaches suggest Tyr is under weighted in the prediction algorithm due to the absence of this residue in the positive training dataset.A combination of methods better defines the score range that discriminates a functional PTS1. In vitro binding to the PEX5 receptor could discriminate amongst strong targeting signals whilst in vivo targeting assays were more sensitive, allowing detection of weak functional import signals that were below the limit of detection in the binding assay. Together the data provide a comprehensive assessment of the factors driving PTS1 efficacy and provide a framework for the more quantitative assessment of the protein import pathway in higher plants.

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“…Observations made for the Hansenula polymorpha Pex5p by fluorescence analysis revealed that the protein is a monomer at pH 6.0 and a tetramer at pH 7.2 (55, 56). According to SEC and SDS- PAGE under non-reducing conditions, Pex5p of Leishmania donovani and Pichia pastoris forms a tetramer of two dimers (57,58). Thus, the unusual migration behavior of yeast Pex5p upon SEC in light of the clear indication that the protein is monomeric by light scattering adds to the peculiar behavior of Pex5p from other species, and in analogy to its human orthologue it is best explained by the assumption that yeast Pex5p is monomeric with an unfolded N-terminal half.…”

Section: Discussionmentioning

confidence: 99%

Structural Insights into Cargo Recognition by the Yeast PTS1 Receptor

Hagen

Drepper

Fischer

et al. 2015

Journal of Biological Chemistry

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Background: Peroxisomal proteins are recognized in the cytosol by the import receptor Pex5p. Results: Photo-cross-linking and mass spectrometry reveal the binding interface of Pex5p and its cargo protein Pcs60p. Conclusion: Pex5p-cargo interaction extends beyond signal sequence recognition and exhibits a bivalent binding mode. Significance: These data indicate a two-step concept of peroxisomal cargo recognition with initial tethering and subsequent lock-in.

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Redox-regulated Cargo Binding and Release by the Peroxisomal Targeting Signal Receptor, Pex5

Cited by 71 publications

References 39 publications

The Leishmania donovani peroxin 14 binding domain accommodates a high degeneracy in the pentapeptide motifs present on peroxin 5

The Leishmania donovani peroxin 14 binding domain accommodates a high degeneracy in the pentapeptide motifs present on peroxin 5

Experimental Validation of Plant Peroxisomal Targeting Prediction Algorithms by Systematic Comparison of In Vivo Import Efficiency and In Vitro PTS1 Binding Affinity

Structural Insights into Cargo Recognition by the Yeast PTS1 Receptor

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