The RING-type ubiquitin ligases Pex2p, Pex10p and Pex12p form a heteromeric complex that displays enhanced activity in an ubiquitin conjugating enzyme-selective manner.

The RING finger peroxins Pex2p, Pex10p and Pex12p are central components of the peroxisomal matrix protein import machinery. The RING domain enables each of these proteins to exhibit ubiquitin-protein ligase activity, which has been linked to ubiquitin-dependent regulation of the peroxisomal import receptor Pex5p. The RING peroxins are considered to ...
form a heteromeric complex in vivo, although the elucidation of the structural assembly, as well as the functional interplay of the RING domains, has remained elusive. Using in vitro approaches, we show that the RING domains form a heteromeric complex with Pex10p(RING) as a central component that directly binds the Pex2p(RING) and Pex12p(RING). The RING domains proved to function as heteromeric pairs that display an Pex10p-dependent enhanced ligase activity in an ubiquitin conjugating enzyme-selective manner.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Escherichia coli, Molecular Sequence Data, Peroxisomes, Protein Binding, Protein Multimerization, RING Finger Domains, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Ubiquitin, Ubiquitin-Conjugating Enzymes, Ubiquitination
FEBS J.
Date: Jun. 01, 2012
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