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In vitro synthesized bacterial outer membrane protein is integrated into bacterial inner membranes but translocated across microsomal membranes.

Abstract：

:The LamB protein is an integral membrane protein of the outer membrane of Escherichia coli. We have now found that, when synthesized in an E. coli cell-free translation system supplemented with inverted vesicles derived from the E. coli inner membrane, LamB protein is integrated into the vesicle membrane as assayed by its resistance to extraction at alkaline pH. These data suggest that the inner membrane is the primary site for integration of LamB protein prior to subsequent sorting to the outer membrane. When synthesized in a wheat germ cell-free translation system supplemented with canine microsomal membranes, LamB protein is glycosylated at one or two cryptic sites, and surprisingly, it is translocated across instead of being integrated into the vesicle membrane. We suggest that the translocation machinery of the microsomal membrane, although able to recognize the signal sequence(s) of LamB, is unable to recognize its stop-transfer sequence(s), thereby yielding translocation instead of integration.

journal_name

Nature

journal_title

Nature

authors

Watanabe M,Hunt JF,Blobel G

doi

10.1038/323071a0

subject

Has Abstract

pub_date

1986-09-04 00:00:00

pages

71-3

issue

6083

eissn

0028-0836

issn

1476-4687

journal_volume

323

pub_type

杂志文章

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