title: Membrane protein topology: effects of delta mu H+ on the translocation of charged residues explain the 'positive inside' rule.
abstract: The membrane electrochemical potential is critical for the export of most periplasmic proteins in Escherichia coli. Its exact role during insertion of integral inner membrane proteins, however, remains obscure. Using derivatives of the inner membrane protein leader peptidase (Lep), we now show that the membrane potential appears to stimulate the membrane translocation of chain segments containing negatively charged residues, that positively charged regions appear to be more easily translocated in the absence of a potential, and that certain Lep constructs insert with different topologies in the presence and absence of a membrane potential, suggesting that the electrochemical potential introduces an asymmetry between the topological effects of positively and negatively charged amino acids during the process of membrane protein insertion in E. coli.
authors.affiliation: Karolinska Institute Center for Structural Biochemistry, NOVUM, Huddinge, Sweden.
authors.forename: H
authors.initials: H
authors.lastname: Andersson
authors.forename: G
authors.initials: G
authors.lastname: von Heijne
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001693:Biological Transport, Active / Q000235:genetics; D010450:Endopeptidases / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000502:physiology*; D008564:Membrane Potentials; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D008954:Models, Biological; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011522:Protons; D011994:Recombinant Proteins / Q000378:metabolism; D012697:Serine Endopeptidases; D013329:Structure-Activity Relationship
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D011522:Protons; D011994:Recombinant Proteins; D010450:Endopeptidases; D012697:Serine Endopeptidases; C026515:type I signal peptidase