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J. Biol. Chem., Vol. 276, Issue 29, 27266-27271, July 20, 2001
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From the Archaebacteria thrive in environments
characterized by anaeobiosis, saturated salt, and both high and low
extremes of temperature and pH. The bulk of their membrane lipids are
polar, characterized by the archaeal structural features typified by
ether linkage of the glycerol backbone to isoprenoid chains of constant
length, often fully saturated, and with sn-2,3
stereochemistry opposite that of glycerolipids of Bacteria and Eukarya.
Also unique to these bacteria are macrocyclic archaeol and membrane
spanning caldarchaeol lipids that are found in some extreme
thermophiles and methanogens. To define the barrier function of
archaebacterial membranes and to examine the effects of these unique
structural features on permeabilities, we investigated the water,
solute (urea and glycerol), proton, and ammonia permeability of
liposomes formed by these lipids. Both the macrocyclic archaeol and
caldarchaeol lipids reduced the water, ammonia, urea, and
glycerol permeability of liposomes significantly (6-120-fold) compared
with diphytanylphosphatidylcholine liposomes. The presence of the ether
bond and phytanyl chains did not significantly affect these
permeabilities. However, the apparent proton permeability was reduced
3-fold by the presence of an ether bond. The presence of macrocyclic
archaeol and caldarchaeol structures further reduced apparent proton
permeabilities by 10-17-fold. These results indicate that the limiting
mobility of the midplane hydrocarbon region of the membranes formed by
macrocyclic archaeol and caldarchaeol lipids play a significant role in
reducing the permeability properties of the lipid membrane. In
addition, it appears that substituting ether for ester bonds presents
an additional barrier to proton flux.
Molecular Mechanisms of Water and Solute Transport across
Archaebacterial Lipid Membranes*
§,
Renal-Electrolyte Division, Department of
Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania 15261 and the ¶ Institute of Biological Sciences, National Research
Council, Ottawa, Ontario K1A OR6, Canada
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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