B. Tolner et al., ADAPTATION OF MICROORGANISMS AND THEIR TRANSPORT-SYSTEMS TO HIGH-TEMPERATURES, Comparative biochemistry and physiology. Section A: Comparative physiology, 118(3), 1997, pp. 423-428
Citations number
31
Categorie Soggetti
Physiology,Biology
Journal title
Comparative biochemistry and physiology. Section A: Comparative physiology
Growth of Bacteria and Archaea has been observed at temperatures up to
95 and 110 degrees C, respectively. These thermophiles are adapted to
environments of high temperature by changes in the membrane lipid com
position, higher thermostabilities of the (membrane) proteins, higher
turnover rates of the energy transducing enzymes, and/or the (exclusiv
e) use of sodium-ions rather than protons as coupling ion in energy tr
ansduction. The proton permeability of the cytoplasmic membrane of bac
teria and archaea was observed to increase with the temperature. This
increased proton permeability limits the maximum temperature of growth
of bacteria. Higher growth temperatures can be reached by an increase
d proton pumping activity by using the less permeable sodium ions as c
oupling ions or by changing the lipid composition of the cytoplasmic m
embrane. The Na+/H+/glutamate transport proteins of the thermophiles B
acillus stearothermophilus (GltT(Bc)) and Bacillus caldotenax (GltT(Bc
)) were studied extensively. These transportproteins have unique featu
res. Transport of L-glutamate occurs in symport with 1 Na+ and 1 H+ wh
en the transport proteins are expressed in their natural environment.
The sodium ion dependency of the GltT transporters of these Bacillus s
trains was found to increase with temperature. However, when the GltT
proteins are expressed in the mesophile Escherichia coli, electrogenic
symport of L-glutamate occurs with greater than or equal to 2 H+. The
se observations suggest that the conformation of the transport protein
s in the E. coli and the Bacillus membranes differs, and that the conf
ormation influences the coupling ion selectivity. The Na+/H+/glutamate
transport proteins of B. stearothermophilus (GltT(Bc)) and B. caldote
nax (GltT(Bc)) are homologous to transport systems of glutamate and st
ructurally related compounds from mesophilic organisms. Both sodium, a
s well as proton coupled transporters, belong to this family of carbox
ylate transporters (FCT). (C) 1997 Elsevier Science Inc.