Outer membrane protein A of Escherichia coli forms temperature-sensitive channels in planar lipid bilayers.
The temperature dependence of single-channel conductance and open probability for outer membrane protein A (OmpA) of Escherichia coli were examined in planar lipid bilayers. OmpA formed two interconvertible conductance states, small channels, 36-140 pS, between 15 and 37 degrees C, and large channels, 115-373 pS, between 21 and 39 degrees C. Increasing temperatures had strong effects on open probabilities and on the ratio of large to small channels, particularly between 22 and 34 degrees C, which effected sharp increases in average conductance. The data infer that OmpA is a flexible temperature-sensitive protein that exists as a small pore structure at lower temperatures, but refolds into a large pore at higher temperatures.
Zakharian
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Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, USA.
Reusch
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D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D004553:Electric Conductivity; D004563:Electrochemistry; D004926:Escherichia coli / Q000378:metabolism*; D007473:Ion Channels / Q000737:chemistry / Q000378:metabolism*; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism*; D013696:Temperature
D001425:Bacterial Outer Membrane Proteins; D007473:Ion Channels; D008051:Lipid Bilayers; C078167:OMPA outer membrane proteins