A large-conductance mechanosensitive channel in E. coli encoded by mscL alone

Sergel I. Sukharev, Paul Blount, Boris Martinac, Frederick R. Blattner, Ching Kung

Research output: Contribution to journalArticlepeer-review

534 Scopus citations

Abstract

ALL cellular organisms respond to vibration, touch, gravity or changes in osmolarity, although the molecules on which such mechanosensations depend are unknown. Candidates include certain channels that gate in response to membrane stretch1,2. Patch-clamp experiments with Escherichia coli envelope have revealed a mechanosensitive channel with very large conductance (MscL) and one with a smaller conductance (MscS)3-6 which may be important in osmoregulation. Here we have solubilized and fractionated the envelope, reconstituted the MscL activity in vitro, and traced it to a small protein, whose gene, mscL, we then cloned. Insertional disruption of mscL removes the channel activity, whereas re-expression of mscL borne on an expression plasmid restores it. MscL-channel activities were observed in material from a cell-free expression system with mscL as the only template. The mscL nucleotide sequence predicts a unique protein of only 136 amino acids, with a highly hydrophobic core and very different from porins or other known proteins.

Original languageEnglish (US)
Pages (from-to)265-268
Number of pages4
JournalNature
Volume368
Issue number6468
DOIs
StatePublished - Jan 1 1994

ASJC Scopus subject areas

  • General

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