In vitro assembly of the functional porin trimer from dissociated monomers in Pseudomonas aeruginosa

E. Yoshihara, H. Yoneyama, T. Nakae

研究成果: Article査読

22 被引用数 (Scopus)

抄録

The molecular weights of monomeric and oligomeric forms of the newly identified porins, protein D2, of the outer membrane of Pseudomonas aeruginosa appeared to be 47,000 and 137,000, respectively, as determined by the light scattering technique. Presence of the trimeric aggregates of the homologous subunits in the intact outer membrane, the liposome membrane, and the non-ionic surfactant were confirmed through cross-linking experiments and immunoblotting techniques. The protein D2 monomers prepared in 0.1 % of sodium dodecyl sulfate at 23 °C spontaneously reassembled into the trimeric aggregate when the surfactant dropped below critical concentration. The diffusion rates of saccharides and β-lactam antibiotics through the liposome membranes reconstituted from the reassembled protein D2 trimers were indistinguishable from those of the native protein D2. This study shed some light on the porin trimer assembly as well as on the mechanism of carbapenem diffusion through the protein D2 pores.

本文言語English
ページ(範囲)952-957
ページ数6
ジャーナルJournal of Biological Chemistry
266
2
出版ステータスPublished - 1991
外部発表はい

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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