Translocation of a functional protein by a voltage-dependent ion channel.

Abstract:

:The voltage-dependent gating of the colicin channel involves a substantial structural rearrangement that results in the transfer of about 35% of the 200 residues in its pore-forming domain across the membrane. This transfer appears to represent an unusual type of protein translocation that does not depend on a large, multimeric, protein pore. To investigate the ability of this system to transport arbitrary proteins, we made use of a pair of strongly interacting proteins, either of which could serve as a translocated cargo or as a probe to detect the other. Here we show that both an 86-residue and a 134-residue hydrophilic protein inserted into the translocated segment of colicin A are themselves translocated and are functional on the trans side of the bilayer. The disparate features of these proteins suggest that the colicin channel has a general protein translocation mechanism.

authors

Slatin SL,Nardi A,Jakes KS,Baty D,Duché D

doi

10.1073/pnas.022480199

keywords:

subject

Has Abstract

pub_date

2002-02-05 00:00:00

pages

1286-91

issue

3

eissn

0027-8424

issn

1091-6490

pii

99/3/1286

journal_volume

99

pub_type

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