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

E. Yoshihara, H. Yoneyama, T. Nakae

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)952-957
Number of pages6
JournalJournal of Biological Chemistry
Volume266
Issue number2
Publication statusPublished - 1991
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'In vitro assembly of the functional porin trimer from dissociated monomers in Pseudomonas aeruginosa'. Together they form a unique fingerprint.

Cite this