The cytoplasmic membrane of bacteria is a selective barrier that restr
icts entry and exit of solutes. Transport of solutes across this membr
ane is catalyzed by specific membrane proteins. Integral membrane prot
eins usually require specific lipids for optimal activity and are inhi
bited by other lipid species. Their activities are also sensitive to t
he lipid bilayer dynamics and physico-chemical state. Bacteria can ada
pt to changes in the environments (respective temperature, hydrostatic
pressure, and pH) by altering the lipid composition of the membrane.
Homeoviscous adaptation results in the maintenance of the liquid-cryst
alline phase through alterations in the degree of acyl chain saturatio
n and branching, acyl chain length and the sterol content of the membr
ane. Homeophasic adaptation prevents the formation of non-bilayer phas
es, which would disrupt membrane organization and increase permeabilit
y. A balance is maintained between the lamellar phase, preferring lipi
ds, and those that adopt a non-bilayer organization. As a result, the
membrane proteins are optimally active under physiological conditions.
The molecular basis of lipid-protein interactions is still obscure. A
nnular lipids stabilize integral membrane proteins. Stabilization occu
rs through electrostatic and possibly other interactions between the l
ipid headgroups and the charged amino acid residues close to the phosp
holipid-water interface, and hydrophobic interactions between the fatt
y acyl chains and the membrane-spanning segments. Reconstitution techn
iques allow manipulation of the lipid composition of the membrane in a
way that is difficult to achieve in vivo. The physical characteristic
s of membrane lipids that affect protein-mediated transport functions
have been studied in liposomal systems that separate an inner and oute
r compartment. The activity of most transport proteins is modulated by
the bulk physical characteristics of the lipid bilayer, while specifi
c lipid requirements appear rare.