PEROXISOME ASSEMBLY FACTOR-II, A PUTATIVE ATPASE CLONED BY FUNCTIONALCOMPLEMENTATION ON A PEROXISOME-DEFICIENT MAMMALIAN-CELL MUTANT

Rat peroxisome assembly factor-2 (PAF-2) cDNA was isolated by function al complementation of peroxisome deficiency of a mutant CHO cell line, ZP92, using transient transfection assay. This cDNA encodes a 978-ami no acid protein with two putative ATP-binding sites. PAF-2 is a member of a putative ATPase family, including two yeast gene products essent ial for peroxisome assembly. A stable transformant of ZP92 with the cD NA was morphologically and biochemically restored for peroxisome bioge nesis. Fibroblasts derived from patients deficient in peroxisome bioge nesis (complementation group C) were also complemented with PAF-2 cDNA , indicating that PAF-2 is a strong candidate for the pathogenic gene of group C peroxisome deficiency.