THE HANSENULA-POLYMORPHA PER1 GENE IS ESSENTIAL FOR PEROXISOME BIOGENESIS AND ENCODES A PEROXISOMAL MATRIX PROTEIN WITH BOTH CARBOXY-TERMINAL AND AMINO-TERMINAL TARGETING SIGNALS

Citation
Hr. Waterham et al., THE HANSENULA-POLYMORPHA PER1 GENE IS ESSENTIAL FOR PEROXISOME BIOGENESIS AND ENCODES A PEROXISOMAL MATRIX PROTEIN WITH BOTH CARBOXY-TERMINAL AND AMINO-TERMINAL TARGETING SIGNALS, The Journal of cell biology, 127(3), 1994, pp. 737-749
Citations number
65
Categorie Soggetti
Cytology & Histology
Journal title
ISSN journal
00219525
Volume
127
Issue
3
Year of publication
1994
Pages
737 - 749
Database
ISI
SICI code
0021-9525(1994)127:3<737:THPGIE>2.0.ZU;2-J
Abstract
We describe the cloning of the Hansenula polymorpha PER1 gene and the characterization of the gene and its product, PER1p. The gene was clon ed by functional complementation of a per1 mutant of H. polymorpha, wh ich was impaired in the import of peroxisomal matrix proteins (Pim(-) phenotype). The DNA sequence of PER1 predicts that PER1p is a polypept ide of 650 amino acids with no significant sequence similarity to othe r known proteins. PER1 expression was low but significant in wild-type H. polymorpha growing on glucose and increased during growth on any o ne of a number of substrates which induce peroxisome proliferation. PE R1p contains both a carboxy- (PTS1) and an amino-terminal (PTS2) perox isomal targeting signal which both were demonstrated to be capable of directing bacterial beta-lactamase to the organelle. In wild-type H. p olymorpha PER1p is a protein of low abundance which was demonstrated t o be localized in the peroxisomal matrix. Our results suggest that the import of PER1p into peroxisomes is a prerequisite for the import of additional matrix proteins and we suggest a regulatory function of PER 1p on peroxisomal protein import.