Faculty, Staff and Student Publications
Lipid-Protein Interactions Drive Membrane Protein Topogenesis in Accordance with the Positive Inside Rule*
Publication Date
4-10-2009
Journal
The Journal of Biological Chemistry
Abstract
Transmembrane domain orientation within some membrane proteins is dependent on membrane lipid composition. Initial orientation occurs within the translocon, but final orientation is determined after membrane insertion by interactions within the protein and between lipid headgroups and protein extramembrane domains. Positively and negatively charged amino acids in extramembrane domains represent cytoplasmic retention and membrane translocation forces, respectively, which are determinants of protein orientation. Lipids with no net charge dampen the translocation potential of negative residues working in opposition to cytoplasmic retention of positive residues, thus allowing the functional presence of negative residues in cytoplasmic domains without affecting protein topology.
Keywords
Amino Acids, Biochemistry, Cell Membrane, Cytoplasm, Escherichia coli, Escherichia coli Proteins, Lipid Bilayers, Lipids, Membrane Proteins, Membrane Transport Proteins, Models, Biological, Protein Conformation, Protein Engineering, Protein Transport
DOI
10.1074/jbc.R800081200
PMID
19074771
PMCID
PMC2665083
PubMedCentral® Posted Date
April 2009
PubMedCentral® Full Text Version
Post-print
Published Open-Access
yes