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Biophys J, January 2001, p. 229-240, Vol. 80, No. 1
Department of Pharmacology, QEII Medical Center, The University of Western Australia, Nedlands WA 6907, Australia
The TM1 domain of the large conductance mechanosensitive
(MS) channel of Escherichia coli was used as a genetic
probe to search the genomic database of the archaeon
Methanoccoccus jannashii for MscL homologs. We report
that the hypothetical protein MJ0170 of M. jannashii
exhibited 38.5% sequence identity with the TM1 domain of Eco-MscL.
Moreover, MJ0170 was found to be a conserved homolog of MscS, the
second type of E. coli MS channel encoded by the
yggB gene. Furthermore, we identified a cluster of
charged residues KIKEE in the C-terminus of MJ0170 that strikingly
resembled the charged C-terminal amino acid cluster present in Eco-MscL (RKKEE). We cloned and expressed MJ0170 in E. coli,
which when reconstituted into liposomes or expressed in the cell
membrane of giant E. coli spheroplasts, exhibited
similar activity to the bacterial MS channels. Our study suggests that
the M. jannashii MS channel and its homologs evolved as
a result of gene duplication of the ancestral MscL-like molecule with
the TM1 domain remaining the most conserved structural motif among
prokaryotic MS channels.
Biophys J, January 2001, p. 229-240, Vol. 80, No. 1
© 2001 by the Biophysical Society 0006-3495/01/01/229/12 $2.00
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