Two families of mechanosensitive channel proteins

C. D. Pivetti, M. R. Yen, Samantha Miller, W. Busch, Y. H. Tseng, Ian Rylance Booth, M. H.,Jr Saier

Research output: Contribution to journalEditorial

156 Citations (Scopus)

Abstract

Mechanosensitive (MS) channels that provide protection against hypoosmotic shock are found in the membranes of organisms from the three domains of life: bacteria, archaea, and eucarya. Two families of ubiquitous MS channels are recognized, and these have been designated the MscL and MscS families. A high-resolution X-ray crystallographic structure is available for a member of the MscL family, and extensive molecular genetic, biophysical, and biochemical studies conducted in many laboratories have allowed postulation of a gating mechanism allowing the interconversion of a tightly closed state and an open state that controls transmembrane ion and metabolite fluxes. In contrast to the MscL channel proteins, which are of uniform topology, the much larger MscS family includes protein members with topologies that are predicted to vary from 3 to 11 alpha-helical transmembrane segments (TMSs) per polypeptide chain. Sequence analyses reveal that the three C-terminal TMSs of MscS channel proteins are conserved among family members and that the third of these three TMSs exhibits a 20-residue motif that is shared by the channel-forming TMS (TMS 1) of the MscL proteins. We propose that this C-terminal TMS in MscS family homologues serves as the channel-forming helix in a homooligomeric structure. The presence of a conserved residue pattern for the putative channel-forming TMSs in the MscL and MscS family proteins suggests a common structural organization, gating mechanism, and evolutionary origin.

Original languageEnglish
Pages (from-to)66-85, table of contents
Number of pages22
JournalMicrobiology and Molecular Biology Reviews : MMBR
Volume67
Issue number1
DOIs
Publication statusPublished - 2003

Keywords

  • ESCHERICHIA-COLI
  • ION CHANNELS
  • GATING MECHANISM
  • MYCOBACTERIUM-TUBERCULOSIS
  • MEMBRANE-PROTEINS
  • SINGLE RESIDUE
  • PATCH-CLAMP
  • MSCL
  • TOPOLOGY
  • MUTATIONS

Cite this

Pivetti, C. D., Yen, M. R., Miller, S., Busch, W., Tseng, Y. H., Booth, I. R., & Saier, M. H. J. (2003). Two families of mechanosensitive channel proteins. Microbiology and Molecular Biology Reviews : MMBR, 67(1), 66-85, table of contents. https://doi.org/10.1128/MMBR.67.1.66-85.2003

Two families of mechanosensitive channel proteins. / Pivetti, C. D.; Yen, M. R.; Miller, Samantha; Busch, W.; Tseng, Y. H.; Booth, Ian Rylance; Saier, M. H.,Jr.

In: Microbiology and Molecular Biology Reviews : MMBR, Vol. 67, No. 1, 2003, p. 66-85, table of contents.

Research output: Contribution to journalEditorial

Pivetti, CD, Yen, MR, Miller, S, Busch, W, Tseng, YH, Booth, IR & Saier, MHJ 2003, 'Two families of mechanosensitive channel proteins', Microbiology and Molecular Biology Reviews : MMBR, vol. 67, no. 1, pp. 66-85, table of contents. https://doi.org/10.1128/MMBR.67.1.66-85.2003
Pivetti, C. D. ; Yen, M. R. ; Miller, Samantha ; Busch, W. ; Tseng, Y. H. ; Booth, Ian Rylance ; Saier, M. H.,Jr. / Two families of mechanosensitive channel proteins. In: Microbiology and Molecular Biology Reviews : MMBR. 2003 ; Vol. 67, No. 1. pp. 66-85, table of contents.
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AU - Pivetti, C. D.

AU - Yen, M. R.

AU - Miller, Samantha

AU - Busch, W.

AU - Tseng, Y. H.

AU - Booth, Ian Rylance

AU - Saier, M. H.,Jr

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N2 - Mechanosensitive (MS) channels that provide protection against hypoosmotic shock are found in the membranes of organisms from the three domains of life: bacteria, archaea, and eucarya. Two families of ubiquitous MS channels are recognized, and these have been designated the MscL and MscS families. A high-resolution X-ray crystallographic structure is available for a member of the MscL family, and extensive molecular genetic, biophysical, and biochemical studies conducted in many laboratories have allowed postulation of a gating mechanism allowing the interconversion of a tightly closed state and an open state that controls transmembrane ion and metabolite fluxes. In contrast to the MscL channel proteins, which are of uniform topology, the much larger MscS family includes protein members with topologies that are predicted to vary from 3 to 11 alpha-helical transmembrane segments (TMSs) per polypeptide chain. Sequence analyses reveal that the three C-terminal TMSs of MscS channel proteins are conserved among family members and that the third of these three TMSs exhibits a 20-residue motif that is shared by the channel-forming TMS (TMS 1) of the MscL proteins. We propose that this C-terminal TMS in MscS family homologues serves as the channel-forming helix in a homooligomeric structure. The presence of a conserved residue pattern for the putative channel-forming TMSs in the MscL and MscS family proteins suggests a common structural organization, gating mechanism, and evolutionary origin.

AB - Mechanosensitive (MS) channels that provide protection against hypoosmotic shock are found in the membranes of organisms from the three domains of life: bacteria, archaea, and eucarya. Two families of ubiquitous MS channels are recognized, and these have been designated the MscL and MscS families. A high-resolution X-ray crystallographic structure is available for a member of the MscL family, and extensive molecular genetic, biophysical, and biochemical studies conducted in many laboratories have allowed postulation of a gating mechanism allowing the interconversion of a tightly closed state and an open state that controls transmembrane ion and metabolite fluxes. In contrast to the MscL channel proteins, which are of uniform topology, the much larger MscS family includes protein members with topologies that are predicted to vary from 3 to 11 alpha-helical transmembrane segments (TMSs) per polypeptide chain. Sequence analyses reveal that the three C-terminal TMSs of MscS channel proteins are conserved among family members and that the third of these three TMSs exhibits a 20-residue motif that is shared by the channel-forming TMS (TMS 1) of the MscL proteins. We propose that this C-terminal TMS in MscS family homologues serves as the channel-forming helix in a homooligomeric structure. The presence of a conserved residue pattern for the putative channel-forming TMSs in the MscL and MscS family proteins suggests a common structural organization, gating mechanism, and evolutionary origin.

KW - ESCHERICHIA-COLI

KW - ION CHANNELS

KW - GATING MECHANISM

KW - MYCOBACTERIUM-TUBERCULOSIS

KW - MEMBRANE-PROTEINS

KW - SINGLE RESIDUE

KW - PATCH-CLAMP

KW - MSCL

KW - TOPOLOGY

KW - MUTATIONS

U2 - 10.1128/MMBR.67.1.66-85.2003

DO - 10.1128/MMBR.67.1.66-85.2003

M3 - Editorial

VL - 67

SP - 66-85, table of contents

JO - Microbiology and Molecular Biology Reviews : MMBR

JF - Microbiology and Molecular Biology Reviews : MMBR

SN - 1092-2172

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