A large-conductance mechanosensitive channel in E. coli encoded by mscL alone (original) (raw)

Nature volume 368, pages 265–268 (1994)Cite this article

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.

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Author notes

  1. Boris Martinac
    Present address: Department of Pharmacology, The University of Western Australia, Nedlands, Perth, Western Australia, 6009, Australia
  2. Ching Kung: To whom correspondence should be addressed

Authors and Affiliations

  1. Laboratory of Molecular Biology,
    Sergei I. Sukharev, Paul Blount, Boris Martinac & Ching Kung
  2. Department of Genetics, University of Wisconsin-Madison, 1525 Linden Drive, Madison, Wisconsin, 53706, USA
    Frederick R. Blattner & Ching Kung

Authors

  1. Sergei I. Sukharev
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  2. Paul Blount
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  3. Boris Martinac
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  4. Frederick R. Blattner
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  5. Ching Kung
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Sukharev, S., Blount, P., Martinac, B. et al. A large-conductance mechanosensitive channel in E. coli encoded by mscL alone.Nature 368, 265–268 (1994). https://doi.org/10.1038/368265a0

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