BIOMAT Database Logo BIOMAT Database Logo

The Hansenula polymorpha PER3 gene is essential for the import of PTS1 proteins into the peroxisomal matrix. 1995

I J van der Klei, and R E Hilbrands, and G J Swaving, and H R Waterham, and E G Vrieling, and V I Titorenko, and J M Cregg, and W Harder, and M Veenhuis
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Haren, The Netherlands.

PER genes are essential for the assembly of peroxisomes in Hansenula polymorpha. Here we describe the PER3 gene which was cloned by functional complementation of a H. polymorpha per3 mutant. The complementing PER3 gene encodes a protein of 569 amino acids (Per3p) with a calculated mass of 63.9 kDa; Per3p belongs to the tetratricopeptide repeat protein family and is located in both the cytosol and the peroxisomal matrix. Remarkably, Per3p does not contain a known targeting signal (PTS1 or PTS2). The PER3 gene product shows similarity to the Saccharomyces cerevisiae Pas10p (40% identity) and the Pichia pastoris Pas8p (55% identity). However, their function apparently cannot be interchanged since the P. pastoris PAS8 gene failed to functionally complement a H. polymorpha per3 disruption mutant. The per3 disruption mutant contained normal but small peroxisomes in which PTS2 proteins (both homologous and heterologous) were imported. Other matrix proteins (in particular PTS1 proteins) resided in the cytosol where they were normally assembled and active. We argue that Per3p is a component of the peroxisomal import machinery and most probably shuttles matrix proteins from the cytosol to the organellar matrix.

UI MeSH Term Description Entries
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D008830 Microbodies Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes. Glycosomes,Glycosome,Microbody
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010843 Pichia Yeast-like ascomycetous fungi of the family Saccharomycetaceae, order SACCHAROMYCETALES isolated from exuded tree sap. Hansenula,Hansenulas,Pichias
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D005656 Fungal Proteins Proteins found in any species of fungus. Fungal Gene Products,Fungal Gene Proteins,Fungal Peptides,Gene Products, Fungal,Yeast Proteins,Gene Proteins, Fungal,Peptides, Fungal,Proteins, Fungal
D005800 Genes, Fungal The functional hereditary units of FUNGI. Fungal Genes,Fungal Gene,Gene, Fungal
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D001692 Biological Transport The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments. Transport, Biological,Biologic Transport,Transport, Biologic

Related Publications

I J van der Klei, and R E Hilbrands, and G J Swaving, and H R Waterham, and E G Vrieling, and V I Titorenko, and J M Cregg, and W Harder, and M Veenhuis
Import of assembled PTS1 proteins into peroxisomes of the yeast Hansenula polymorpha: yes and no!
August 2002, Biochimica et biophysica acta,
I J van der Klei, and R E Hilbrands, and G J Swaving, and H R Waterham, and E G Vrieling, and V I Titorenko, and J M Cregg, and W Harder, and M Veenhuis
Peroxisomal matrix protein import. Suppression of protein import defects in Hansenula polymorpha pex mutants by overproduction of the PTS1 receptor Pex5p.
January 2000, Cell biochemistry and biophysics,
I J van der Klei, and R E Hilbrands, and G J Swaving, and H R Waterham, and E G Vrieling, and V I Titorenko, and J M Cregg, and W Harder, and M Veenhuis
The deubiquitination of the PTS1-import receptor Pex5p is required for peroxisomal matrix protein import.
February 2019, Biochimica et biophysica acta. Molecular cell research,
I J van der Klei, and R E Hilbrands, and G J Swaving, and H R Waterham, and E G Vrieling, and V I Titorenko, and J M Cregg, and W Harder, and M Veenhuis
Hansenula polymorpha Pex19p is essential for the formation of functional peroxisomal membranes.
April 2004, The Journal of biological chemistry,
I J van der Klei, and R E Hilbrands, and G J Swaving, and H R Waterham, and E G Vrieling, and V I Titorenko, and J M Cregg, and W Harder, and M Veenhuis
Import of proteins into the peroxisomal matrix.
September 2013, Frontiers in physiology,
I J van der Klei, and R E Hilbrands, and G J Swaving, and H R Waterham, and E G Vrieling, and V I Titorenko, and J M Cregg, and W Harder, and M Veenhuis
Pex9p is a new yeast peroxisomal import receptor for PTS1-containing proteins.
November 2016, Journal of cell science,
I J van der Klei, and R E Hilbrands, and G J Swaving, and H R Waterham, and E G Vrieling, and V I Titorenko, and J M Cregg, and W Harder, and M Veenhuis
The methylotrophic yeast Hansenula polymorpha contains an inducible import pathway for peroxisomal matrix proteins with an N-terminal targeting signal (PTS2 proteins).
December 1994, Proceedings of the National Academy of Sciences of the United States of America,
I J van der Klei, and R E Hilbrands, and G J Swaving, and H R Waterham, and E G Vrieling, and V I Titorenko, and J M Cregg, and W Harder, and M Veenhuis
Obstruction of polyubiquitination affects PTS1 peroxisomal matrix protein import.
September 2005, Biochimica et biophysica acta,
I J van der Klei, and R E Hilbrands, and G J Swaving, and H R Waterham, and E G Vrieling, and V I Titorenko, and J M Cregg, and W Harder, and M Veenhuis
Distinct Pores for Peroxisomal Import of PTS1 and PTS2 Proteins.
December 2015, Cell reports,
I J van der Klei, and R E Hilbrands, and G J Swaving, and H R Waterham, and E G Vrieling, and V I Titorenko, and J M Cregg, and W Harder, and M Veenhuis
The peroxisomal import signal of amine oxidase from the yeast Hansenula polymorpha is not universal.
April 1992, Yeast (Chichester, England),
Copied contents to your clipboard!