6533b83afe1ef96bd12a7be7
RESEARCH PRODUCT
Anionic Lipids Modulate the Activity of the Aquaglyceroporin GlpF
Dirk SchneiderNoreen KleinNadja Hellmannsubject
AnionsLiposomeMembranesEscherichia coli ProteinsBiophysicsAquaporinBiological membraneBiologyAquaporinsLipidsCell biologyMembraneMembrane proteinNegative chargeLiposomesEscherichia colilipids (amino acids peptides and proteins)Lipid bilayerPotential mechanismdescription
AbstractThe structure and composition of a biological membrane can severely influence the activity of membrane-embedded proteins. Here, we show that the E. coli aquaglyceroporin GlpF has only little activity in lipid bilayers formed from native E. coli lipids. Thus, at first glance, GlpF appears to not be optimized for its natural membrane environment. In fact, we found that GlpF activity was severely affected by negatively charged lipids regardless of the exact chemical nature of the lipid headgroup, whereas GlpF was not sensitive to changes in the lateral membrane pressure. These observations illustrate a potential mechanism by which the activity of an α-helical membrane protein is modulated by the negative charge density around the protein.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2015-08-01 | Biophysical Journal |