Assembly of a cytoplasmic membrane protein in Escherichia coli is dependent on the signal recognition particle.
Targeting of the cytoplasmic membrane protein leader peptidase (Lep) and a Lep mutant (Lep-inv) that inserts with an inverted topology compared to the wild-type protein was studied in Escherichia coli strains that are conditional for the expression of either Ffh or 4.5S RNA, the two components of the E. coli SRP. Depletion of either component strongly affected the insertion of both Lep and Lep-inv into the cytoplasmic membrane. This indicates that SRP is required for the assembly of cytoplasmic membrane proteins in E. coli.
de Gier
J W
JW
Department of Biochemistry, Arrhenius Laboratory, Stockholm University, Sweden.
Mansournia
P
P
Valent
Q A
QA
Phillips
G J
GJ
Luirink
J
J
von Heijne
G
G
D004926:Escherichia coli / Q000201:enzymology*; D008565:Membrane Proteins / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000378:metabolism*; D018271:Signal Recognition Particle / Q000378:metabolism*
D008565:Membrane Proteins; D018271:Signal Recognition Particle; D012697:Serine Endopeptidases; C026515:type I signal peptidase