TY - JOUR
T1 - Monomer-dimer transition of the conserved N-terminal domain of the mammalian peroxisomal matrix protein import receptor, Pex14p
AU - Su, Jian Rong
AU - Takeda, Kazuki
AU - Tamura, Shigehiko
AU - Fujiki, Yukio
AU - Miki, Kunio
N1 - Funding Information:
This work was supported by a Grant for the National Project on Protein Structural and Functional Analyses (to K.M. and Y.F.), Grants-in-Aid for Scientific Research (to Y.F. and K.M.) and a CREST Grant (to Y.F.).
PY - 2010/3/26
Y1 - 2010/3/26
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=77949875332&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77949875332&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2010.02.160
DO - 10.1016/j.bbrc.2010.02.160
M3 - Article
C2 - 20193661
AN - SCOPUS:77949875332
SN - 0006-291X
VL - 394
SP - 217
EP - 221
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -