Context-dependent effects of charged residues in transmembrane segments of MalF-PhoA fusions.
Charged residues were introduced into the C-terminal transmembrane segment of a MalF-PhoA fusion to investigate the efficiency of the altered transmembrane segment to function as an export signal or a stop transfer signal. PhoA assays revealed that charges had negative effects when the transmembrane segment was part of a stop transfer signal but not when it was part of an export signal. Implications of this finding for the biogenesis of polytopic membrane proteins are discussed.
Ehrle
Rainer
R
School of Biosciences, Cardiff University, Cardiff, UK.
Mikhaleva
Natasha
N
Boyd
Dana
D
Davidson
Amy L
AL
Ehrmann
Michael
M
D018528:ATP-Binding Cassette Transporters / Q000378:metabolism; D000469:Alkaline Phosphatase; D001692:Biological Transport; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018844:Cyclin-Dependent Kinases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism; D058619:Maltose-Binding Proteins; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008954:Models, Biological; D009004:Monosaccharide Transport Proteins / Q000378:metabolism
D018528:ATP-Binding Cassette Transporters; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D058619:Maltose-Binding Proteins; D008565:Membrane Proteins; D009004:Monosaccharide Transport Proteins; C461599:maltose transport system, E coli; D018844:Cyclin-Dependent Kinases; D000469:Alkaline Phosphatase; C114089:phoA protein, E coli