Convergence of model systems for peroxisome biogenesis

• Published in: Current opinion in cell biology Vol. 8; no. 4; pp. 513 - 518
• Main Author: Subramani, Suresh
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.08.1996
• Subjects: Biological Transport - genetics; Cell Compartmentation; Humans; Microbodies - metabolism; Models, Biological; Molecular Chaperones - metabolism; Peroxisomal Disorders - genetics; Proteins - metabolism; Receptors, Cytoplasmic and Nuclear - metabolism; PTS1R PTS1 receptor; Pas peroxisome assembly; PXR peroxisome targeting signal receptor; Sc Saccharomyces cerevisiae YlPay peroxisome assembly in Yarrowia lipolytica; Peb peroxisome biogenesis; Per peroxisome; GFP green fluorescent protein; Pp Pichia pastoris; mPTS peroxisomal membrane targeting signal; PMP peroxisomal membrane protein; hsp heat shock protein; PAF peroxisome assembly factor; PTS peroxisomal targeting signal; RCDP rhizomelic chondrodysplasia punctata
• ISSN: 0955-0674; 1879-0410
• DOI: 10.1016/S0955-0674(96)80029-9

Receptors for the two peroxisomal targeting signals PTS1 and PTS2 have recently been identified in yeasts. The disparate subcellular locations of PTS receptor homologs have led to proposals for receptor shuttling between the cytosol and the peroxisomal membrane, and to the suggestion that some of these molecules may even reside normally in the peroxisomal matrix. A peroxisomal membrane protein that interacts with the PTS1 receptor in Saccharomyces cerevisiae may serve as the receptor-docking site on the organelle. The conservation of the PTS1 receptor in several yeasts has led to the cloning and characterization of the gene encoding its human homolog, PTS1R, which is mutated in a group of patients afflicted with fatal peroxisomal disorders. The identification of peroxisome assembly genes in yeasts is likely to lead to the cloning of additional human genes responsible for other generalized peroxisomal disorders. Protein unfolding is not a prerequisite for import of peroxisomal matrix proteins, suggesting novel mechanisms for the translocation of polypeptides across the peroxisomal membrane.