Enlarged Peroxisomes Are Present in Oleic Acid-grown Yarrowia lipolytica Overexpressing the PEX16 Gene Encoding an Intraperoxisomal Peripheral Membrane Peroxin

doi:10.1083/jcb.137.6.1265

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© The Rockefeller University Press, 0021-9525/1997//1265 $5.00
The Journal of Cell Biology, Volume 137, Number 6, , 1997 1265-1278

Article

Enlarged Peroxisomes Are Present in Oleic Acid–grown Yarrowia lipolytica Overexpressing the PEX16 Gene Encoding an Intraperoxisomal Peripheral Membrane Peroxin

Gary A. Eitzen, Rachel K. Szilard, and Richard A. Rachubinski

Department of Cell Biology and Anatomy, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

Pex mutants of the yeast Yarrowia lipolytica are defectivein peroxisome assembly. The mutant strain pex16-1 lacks morphologicallyrecognizable peroxisomes. Most peroxisomal proteins are mislocalized to a subcellular fraction enriched for cytosol in pex16 strains,but a subset of peroxisomal proteins is localized at, or near,wild-type levels to a fraction typically enriched for peroxisomes.The PEX16 gene was isolated by functional complementation ofthe pex16-1 strain and encodes a protein, Pex16p, of 391 aminoacids (44,479 D). Pex16p has no known homologues. Pex16p isa peripheral protein located at the matrix face of the peroxisomalmembrane. Substitution of the carboxylterminal tripeptide Ser-Thr-Leu,which is similar to the consensus sequence of peroxisomal targetingsignal 1, does not affect targeting of Pex16p to peroxisomes. Pex16p is synthesized in wild-type cells grown in glucose-containingmedia, and its levels are modestly increased by growth of cellsin oleic acid–containing medium. Overexpression of thePEX16 gene in oleic acid– grown Y. lipolytica leads tothe appearance of a small number of enlarged peroxisomes, whichcontain the normal complement of peroxisomal proteins at levels approaching those of wild-type peroxisomes.

Abbreviations used in this paper: HA, hemagglutinin; ORF, open reading frame; PNS, postnuclear supernatant; PTS, peroxisomal targeting signal.

G.A. Eitzen is the recipient of a Studentship from the AlbertaHeritage Foundation for Medical Research. R.K. Szilard is therecipient of a Studentship from the Medical Research Council(MRC) of Canada. R.A. Rachubinski is an MRC Scientist and anInternational Research Scholar of the Howard Hughes MedicalInstitute. This work was supported by a grant from the MRCto R.A. Rachubinski.

Please address all correspondence to Richard A. Rachubinski,Department of Cell Biology and Anatomy, University of Alberta,Medical Sciences Building 5-14, Edmonton, Alberta T6G 2H7, Canada.Tel.: (403) 492-9868; Fax: (403) 492-9278; E-mail: rrachubi{at}anat.med.ualberta.ca

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