The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane.

Abstract:

:Trigger factor is a soluble, 63,000 dalton protein of E. coli that stabilizes proOmpA, the precursor form of a major outer-membrane protein, in a conformation competent for in vitro membrane assembly. There is approximately one trigger factor molecule bound to each 70S ribosome isolated from cell extracts in physiological buffers. Trigger factor dissociates from ribosomes in 1.5 M LiCl and reassociates with salt-washed ribosomes in low-salt buffer. Binding is exclusively to the 50S (large) subunit, known to contain the exit domain for nascent polypeptide chains. In addition to its associations with proOmpA and ribosomes, excess trigger factor can compete with the proOmpA-trigger factor complex for a limited number of membrane sites that are essential for translocation of proOmpA. These data suggest a model of trigger factor cycling between the cytoplasm, the ribosome, presecretory proteins, and membrane receptor proteins.

journal_name

Cell

journal_title

Cell

authors

Lill R,Crooke E,Guthrie B,Wickner W

doi

10.1016/0092-8674(88)90116-x

subject

Has Abstract

pub_date

1988-09-23 00:00:00

pages

1013-8

issue

7

eissn

0092-8674

issn

1097-4172

pii

0092-8674(88)90116-X

journal_volume

54

pub_type

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