title: Monomer-dimer transition of the conserved N-terminal domain of the mammalian peroxisomal matrix protein import receptor, Pex14p.
abstract: Pex14p is a central component of the peroxisomal matrix protein import machinery. In the recently determined crystal structure, a characteristic face consisting of conserved residues was found on a side of the conserved N-terminal domain of the protein. The face is highly hydrophobic, and is also the binding site for the WXXXF/Y motif of Pex5p. We report herein the dimerization of the domain in the isolated state. The homo-dimers are in equilibrium with the monomers. The homo-dimers are completely dissociated into monomers by complex formation with the WXXXF/Y motif peptide of Pex5p. A putative dimer model shows the interaction between the conserved face and the PXXP motif of another protomer. The model allows us to discuss the mechanism of the oligomeric transition of the full-length Pex14p modulated by the binding of other peroxins.
authors.affiliation: Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
authors.forename: Jian-Rong
authors.initials: JR
authors.lastname: Su
authors.forename: Kazuki
authors.initials: K
authors.lastname: Takeda
authors.forename: Shigehiko
authors.initials: S
authors.lastname: Tamura
authors.forename: Yukio
authors.initials: Y
authors.lastname: Fujiki
authors.forename: Kunio
authors.initials: K
authors.lastname: Miki
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D008565:Membrane Proteins / Q000737:chemistry*; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D051381:Rats; D012097:Repressor Proteins / Q000737:chemistry*
chemical_list: D008565:Membrane Proteins; C499194:Pex14 protein, rat; D012097:Repressor Proteins