Structural and functional differences between two homologous mechanosensitive channels of Methanococcus jannaschii.
We report the molecular cloning and characterization of MscMJLR, a second type of mechanosensitive (MS) channel found in the archaeon Methanococcus jannaschii. MscMJLR is structurally very similar to MscMJ, the MS channel of M.jannaschii that was identified and cloned first by using the TM1 domain of Escherichia coli MscL as a genetic probe. Although it shares 44% amino acid sequence identity and similar cation selectivity with MscMJ, MscMJLR exhibits other major functional differences. The conductance of MscMJLR of approximately 2 nS is approximately 7-fold larger than the conductance of MscMJ and rectifies with voltage. The channel requires approximately 18 kT for activation, which is three times the amount of energy required to activate MscMJ, but is comparable to the activation energy of Eco-MSCL: Our study indicates that a multiplicity of conductance-wise and energetically well-tuned MS channels in microbial cell membranes may provide for cell survival by the sequential opening of the channels upon challenge with different osmotic cues.
Kloda
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Department of Pharmacology, QEII Medical Centre, The University of Western Australia, Crawley, WA 6009, Australia.
Martinac
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B
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015640:Ion Channel Gating; D007473:Ion Channels / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008081:Liposomes; D017017:Methanococcus / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D011189:Potassium Chloride / Q000378:metabolism; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
D019843:Archaeal Proteins; D007473:Ion Channels; D008081:Liposomes; C426018:MscMJ protein, Methanococcus jannaschii; C426017:MscMJLR protein, Methanococcus jannaschii; D011189:Potassium Chloride