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The SH3 domain of the Saccharomyces cerevisiae peroxisomal membrane protein Pex13p functions as a docking site for Pex5p, a mobile receptor for the import PTS1-containing proteins.
- Source :
-
The Journal of cell biology [J Cell Biol] 1996 Oct; Vol. 135 (1), pp. 97-109. - Publication Year :
- 1996
-
Abstract
- We identified a Saccharomyces cerevisiae peroxisomal membrane protein, Pex13p, that is essential for protein import. A point mutation in the COOH-terminal Src homology 3 (SH3) domain of Pex13p inactivated the protein but did not affect its membrane targeting. A two-hybrid screen with the SH3 domain of Pex13p identified Pex5p, a receptor for proteins with a type I peroxisomal targeting signal (PTS1), as its ligand. Pex13p SH3 interacted specifically with Pex5p in vitro. We determined, furthermore, that Pex5p was mainly present in the cytosol and only a small fraction was associated with peroxisomes. We therefore propose that Pex13p is a component of the peroxisomal protein import machinery onto which the mobile Pex5p receptor docks for the delivery of the selected PTS1 protein.
- Subjects :
- 3-Hydroxyacyl CoA Dehydrogenases metabolism
Acetyl-CoA C-Acetyltransferase analysis
Amino Acid Sequence
Base Sequence
Biological Transport
Catalase metabolism
Cloning, Molecular
Cytosol chemistry
Fibroblasts
Genes, Fungal genetics
Humans
Intracellular Membranes chemistry
Ligands
Membrane Proteins analysis
Membrane Proteins genetics
Microbodies chemistry
Molecular Sequence Data
Peroxisome-Targeting Signal 1 Receptor
Point Mutation
Receptors, Cytoplasmic and Nuclear analysis
Receptors, Cytoplasmic and Nuclear genetics
Recombinant Fusion Proteins metabolism
Sequence Deletion
Membrane Proteins metabolism
Microbodies metabolism
Receptors, Cytoplasmic and Nuclear metabolism
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae Proteins
src Homology Domains genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9525
- Volume :
- 135
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- The Journal of cell biology
- Publication Type :
- Academic Journal
- Accession number :
- 8858166
- Full Text :
- https://doi.org/10.1083/jcb.135.1.97