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Vol. 10, Issue 7, 2163-2173, July 1999
*Institut für Biochemie und Molekularbiologie,
Universität Freiburg, D-79104 Freiburg, Germany; and
The molecular requirements for the translocation of secretory
proteins across, and the integration of membrane proteins into, the
plasma membrane of Escherichia coli were compared. This
was achieved in a novel cell-free system from E. coli
which, by extensive subfractionation, was simultaneously rendered
deficient in SecA/SecB and the signal recognition particle (SRP)
components, Ffh (P48), 4.5S RNA, and FtsY. The integration of two
membrane proteins into inside-out plasma membrane vesicles of E.
coli required all three SRP components and could not be driven
by SecA, SecB, and Institut für Biotechnologie, Forschungszentrum
Jülich, D-52425 Jülich, Germany
µH+. In contrast, these were the
only components required for the translocation of secretory proteins
into membrane vesicles, a process in which the SRP components were
completely inactive. Our results, while confirming previous in vivo
studies, provide the first in vitro evidence for the dependence of the
integration of polytopic inner membrane proteins on SRP in E.
coli. Furthermore, they suggest that SRP and SecA/SecB have
different substrate specificities resulting in two separate targeting
mechanisms for membrane and secretory proteins in E.
coli. Both targeting pathways intersect at the translocation
pore because they are equally affected by a blocked translocation channel.
Corresponding author. E-mail address:
mumatthi{at}ruf.uni-freiburg.de.
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