Monomer-dimer transition of the conserved N-terminal domain of the mammalian peroxisomal matrix protein import receptor, Pex14p

Jian Rong Su, Kazuki Takeda, Shigehiko Tamura, Yukio Fujiki, Kunio Miki

Research output: Contribution to journalArticle

6 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)217-221
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume394
Issue number1
DOIs
Publication statusPublished - Mar 26 2010

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Protein Subunits
Dimerization
Dimers
Monomers
Binding Sites
Peptides
Proteins
Machinery
Crystal structure
Protein Domains

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Monomer-dimer transition of the conserved N-terminal domain of the mammalian peroxisomal matrix protein import receptor, Pex14p. / Su, Jian Rong; Takeda, Kazuki; Tamura, Shigehiko; Fujiki, Yukio; Miki, Kunio.

In: Biochemical and Biophysical Research Communications, Vol. 394, No. 1, 26.03.2010, p. 217-221.

Research output: Contribution to journalArticle

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