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Vol. 11, Issue 6, 2085-2102, June 2000
*Department of Biology, Graduate School of Science, Kyushu
University, Fukuoka 812-8581, Japan; Rat cDNA encoding a 372-amino-acid peroxin was isolated, primarily
by functional complementation screening, using a peroxisome-deficient Chinese hamster ovary cell mutant, ZPG208, of complementation group 17. The deduced primary sequence showed ~25% amino acid identity with the yeast Pex3p, thereby we termed this cDNA rat PEX3 (RnPEX3). Human and Chinese hamster
Pex3p showed 96 and 94% identity to rat Pex3p and had 373 amino acids.
Pex3p was characterized as an integral membrane protein of peroxisomes,
exposing its N- and C-terminal parts to the cytosol. A homozygous,
inactivating missense mutation, G to A at position413, in a codon
(GGA) for Gly138 and resulting in a codon
(GAA) for Glu was the genetic cause of peroxisome
deficiency of complementation group 17 ZPG208. The peroxisome-restoring
activity apparently required the full length of Pex3p, whereas its
N-terminal part from residues 1 to 40 was sufficient to target a fusion
protein to peroxisomes. We also demonstrated that Pex3p binds the
farnesylated peroxisomal membrane protein Pex19p. Moreover, upon
expression of PEX3 in ZPG208, peroxisomal membrane
vesicles were assembled before the import of soluble proteins such as
PTS2-tagged green fluorescent protein. Thus, Pex3p assembles membrane
vesicles before the matrix proteins are translocated.
CREST, Japan Science
and Technology Corporation, Tokyo 170-0013, Japan
Corresponding author. E-mail address:
yfujiscb{at}mbox.nc.kyushu-u.ac.jp.
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