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Cited by 177Fungal and yeast genetics researchCellular transport and secretionAutophagy in Disease and Therapy

The Pichia pastoris peroxisomal protein PAS8p is the receptor for the C-terminal tripeptide peroxisomal targeting signal

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Terlecky, S. R., Nuttley, W. M., McCollum, D., Sock, E., Subramani, S.·1995·The EMBO Journal
DOI 10.1002/j.1460-2075.1995.tb00032.xPMC PMC394437
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Abstract

The peroxisomal targeting signal 1 (PTS1), consisting of a C-terminal tripeptide (SKL and variants), directs polypeptides to the peroxisome matrix in evolutionarily diverse organisms. Previous studies in the methylotrophic yeast Pichia pastoris identified a 68 kDa protein, PAS8p, as a potential component of the PTS1 import machinery. We now report several new properties of this molecule which, taken together, show that it is the peroxisomal PTS1 receptor. (i) PAS8p is localized to and tightly associated with the cytoplasmic side of the peroxisomal membrane, (ii) peroxisomes of wild-type, but not of pas8 delta (null) mutant, P.pastoris cells bind a PTS1-containing peptide (CRYHLKPLQSKL), (iii) CRYHLKPLQSKL can be cross-linked to PAS8p after binding at the peroxisome membrane and (iv) purified PAS8p binds CRYHLKPLQSKL with high affinity (nanomolar dissociation constant). In addition, the tetratricopeptide repeat (TPR) domain of PAS8p is identified as the PTS1 binding region.

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Crossref · 10.1002/j.1460-2075.1995.tb00032.x

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  • In the TPR-containing proteins Hop and PAS8, three or more TPR motifs form a TPR domain that recognizes short stretches of primary amino acid sequence at the COOH termini of their target proteins, −EEVD in Hsp70 and Hsp90 and −SKL in peroxisomal proteins.

    “In the case of two TPR-containing proteins, the Hsp70/Hsp90 organizing protein Hop and the peroxisomal import receptor PAS8, three or more TPR motifs form a TPR domain that recognizes short stretches of primary amino acid sequence at the COOH termini of their target proteins, −EEVD in Hsp70 and Hsp90 and −SKL in peroxisomal proteins, respectively (Terlecky et al. 1995; Scheufler et al. 2000).”

    From Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules (2001) · cites this paper as Terlecky et al. 1995

  • The mechanism of interaction between JIP-1 and the TPR motifs of KLC is similar to that of other TPR domain-containing proteins.

    “Thus, the mechanism of interaction between JIP-1 and the TPR motifs of KLC is similar to that of other TPR domain–containing proteins (Terlecky et al. 1995; Scheufler et al. 2000).”

    From Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules (2001) · cites this paper as Terlecky et al. 1995

  • Three or more TPR motifs of KLC generate an extended surface groove that provides the docking site for the linear JIP-1 (and presumably JIP-2) peptide.

    “it is likely that three or more TPR motifs of KLC generate an extended surface groove that provides the docking site for the linear JIP-1 (and presumably JIP-2) peptide.”

    From Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules (2001) · cites this paper as Terlecky et al. 1995

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Research works printed but not linked: 2

  1. Hines,V. (1992) The mitochondrial protein import machinery of Saccharomyces cerevisiae. In Neupert,W. and Lill,R. (eds), Membrane Biogenesis and Protein Targeting. Elsevier Science Publishers, Amsterdam, The Netherlands, pp. 241-252.
  2. Wiemer,E.A., Nuttley,W.M., Bertolaet,B., Li,X., Francke,U., Wheelock,M.J., Anne,U.K., Johnson,K.R. and Subramani,S. (1995) The human PTS I receptor restores peroxisomal protein-import in cells from patients with fatal peroxisomal disorders. J. Cell Biol., in press. Received on March 3, 1995; revised on May 11, 1995

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Authors
Terlecky, S. R., Nuttley, W. M., McCollum, D., Sock, E., & Subramani, S.
Affiliations
University of California San Diego (US)
ORCID
Venue
The EMBO Journal
Publisher
Springer Science and Business Media LLC
Published
1995-08-01
Volume
14
Issue
15
Pages
3627-3634
ISSN
  • 0261-4189 (ISSN-L)
  • 1460-2075
DOI
10.1002/j.1460-2075.1995.tb00032.x
PMC
PMC394437
OpenAlex
W119049379
Cited by
177
References
48
Citations by year
2026: 3 · 2025: 2 · 2024: 1 · 2023: 2 · 2022: 1 · 2021: 2 · 2020: 3 · 2019: 4 · 2018: 2 · 2017: 4 · 2016: 2 · 2015: 6 · 2014: 1 · 2013: 1 · 2012: 2
FWCI
6.32
Type
journal article
Language
en
Open access
Licence
Locations
  • The EMBO Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Science Foundation (9316018)
  • National Institutes of Health (1f32dk009061-01)
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK-41737, 1 F32 DK09061-01)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Keywords
PTS1, Pichia pastoris, peroxisomal protein import, peroxisomal membrane, tetratricopeptide repeat domain, peroxisomal matrix proteins, protein-protein binding
MeSH terms
Peroxisome-Targeting Signal 1 Receptor, Amino Acid Sequence, Base Sequence, Binding Sites, Cross-Linking Reagents, Cytoplasm, Fungal Proteins, Intracellular Membranes, Kinetics, Membrane Proteins, Microbodies, Molecular Sequence Data, Pichia, Succinimides, Sequence Deletion, Receptors, Cytoplasmic and Nuclear

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