Abstract
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.
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