TY - JOUR
T1 - Functional and structural conservation in the mechanosensitive channel MscL implicates elements crucial for mechanosensation
AU - Woe, Paul C.
AU - Blount, Paul
AU - Kung, Ching
PY - 1998
Y1 - 1998
N2 - mscL encodes a channel in Escherichia coil that is opened by membrane stretch force, probably serving as an osmotic gauge. Sequences more or less similar to mscL are found in other bacteria, but the degree of conserved function has been unclear. We subcloned and expressed these putative homologues in E. coli and examined their products under patch clamp. Here, we show that each indeed encodes a conserved mechanosensitive channel activity, consistent with the interpretation that this is an important and primary function of the protein in a wide range of bacteria. Although similar, channels of different bacteria differ in kinetics and their degree of mechanosensitivity. Comparison of the primary sequence of these proteins reveals two highly conserved regions, corresponding to domains previously shown to be important for the function of the wild-type E. coli channel, and a C-terminal region that is not conserved in all species. This structural conservation is providing insight into regions of this molecule that are vital to its role as a mechanosensitive channel and may have broader implications for the understanding of other mechanosensitive systems.
AB - mscL encodes a channel in Escherichia coil that is opened by membrane stretch force, probably serving as an osmotic gauge. Sequences more or less similar to mscL are found in other bacteria, but the degree of conserved function has been unclear. We subcloned and expressed these putative homologues in E. coli and examined their products under patch clamp. Here, we show that each indeed encodes a conserved mechanosensitive channel activity, consistent with the interpretation that this is an important and primary function of the protein in a wide range of bacteria. Although similar, channels of different bacteria differ in kinetics and their degree of mechanosensitivity. Comparison of the primary sequence of these proteins reveals two highly conserved regions, corresponding to domains previously shown to be important for the function of the wild-type E. coli channel, and a C-terminal region that is not conserved in all species. This structural conservation is providing insight into regions of this molecule that are vital to its role as a mechanosensitive channel and may have broader implications for the understanding of other mechanosensitive systems.
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U2 - 10.1046/j.1365-2958.1998.00821.x
DO - 10.1046/j.1365-2958.1998.00821.x
M3 - Article
C2 - 9632260
AN - SCOPUS:7144257172
SN - 0950-382X
VL - 28
SP - 583
EP - 592
JO - Molecular Microbiology
JF - Molecular Microbiology
IS - 3
ER -