Separation of gate‐ and channel‐forming domains in the pore‐forming protein of the outer membrane of Pseudomonas aeruginosa

FEBS Letters

Nakae, Taiji¹  Yoshihara, Eisaku¹ 

[1] Department of Molecular Life, Science, Tokai University, School of Medicine, Isehara 259-11, Japan

关键词: Channel;    Gate;    Outer membrane;    Porin;    Psedomonas aeruginosa;   

DOI  :  10.1016/0014-5793(92)80826-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The domains of the pore-forming protein responsible for the gate and channel formations were separated and identified in the outer membrane of Pseudomonas aeruginosa. The proteolytic cleavage of the 46K channel protein, protein D2, yielded two major domains with apparent M _r of 27K and 19K. We identified the 27K polypeptide to be the channel-forming domain by an in vitro permeability assay. The channel size of purified 27K domain was indistinguishable from that of native protein D2. Degradation of the 19K domain into small subfragments increases the channel activity about ten times suggesting that the 19K polypeptide forms the gate or cap.

【 授权许可】

Unknown