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.
School of Biosciences, Cardiff University, Cardiff, UK.
Rainer
R
Ehrle
Natasha
N
Mikhaleva
Dana
D
Boyd
Amy L
AL
Davidson
Michael
M
Ehrmann
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