Figure 1

Nucleotide-dependent formation of the Pex1/6p-complex.

(a) Domain organization of Pex1p and Pex6p. Pex1p and Pex6p are type-II AAA-proteins, which both comprise two N-terminal domains (NTDs), a non-conserved first AAA-domain (D1) and a conserved second AAA-domain (D2). Conserved Walker A motifs (A2) for ATP binding and Walker B motifs (B2) for hydrolysis of ATP are located in the D2 domains of both peroxins. The D1 domains comprise only remnants of Walker A and B motifs (A1, B1) with exception of a conserved Walker A motif in Pex1p (A1). (b) HisPex1p and HisPex6p in complex were isolated in the presence of ATP or ADP and isolated complexes were analyzed by size exclusion chromatography. Fractions were separated by SDS-PAGE and stained with Coomassie. In the presence of ATP, Pex6p and Pex1p both peaked at a size of approximately 700 kDa which represents the heterohexameric AAA-complex. Under ADP conditions, Pex1p and Pex6p assembled to the 700 kDa complex with a portion disassembling into monomeric Pex6p and trimeric Pex1p.