Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation.

Abstract:

:The TatA and TatB proteins are essential components of the twin arginine protein translocation pathway in Escherichia coli. C-terminal truncation analysis of the TatA protein revealed that a plasmid-expressed TatA protein shortened by 40 amino acids is still fully competent to support protein translocation. Similar truncation analysis of TatB indicated that the final 30 residues of TatB are dispensable for function. Further deletion experiments with TatB indicated that removal of even 70 residues from its C terminus still allowed significant transport. These results imply that the transmembrane and amphipathic helical regions of TatA and TatB are critical for their function but that the C-terminal domains are not essential for Tat transport activity. A chimeric protein comprising the N-terminal region of TatA fused to the amphipathic and C-terminal domains of TatB supports a low level of Tat activity in a strain in which the wild-type copy of either tatA or tatB (but not both) is deleted.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Lee PA,Buchanan G,Stanley NR,Berks BC,Palmer T

doi

10.1128/jb.184.21.5871-5879.2002

keywords:

subject

Has Abstract

pub_date

2002-11-01 00:00:00

pages

5871-9

issue

21

eissn

0021-9193

issn

1098-5530

journal_volume

184

pub_type

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