The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli.

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Article

The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli.

The Journal of biological chemistry - 5 Apr 1992

Nishiyama K, Mizushima S, Tokuda H

Abstract excerpt

Genes encoding the C- and N-terminal regions of SecE were constructed and placed under the control of the tac promoter on plasmids. The C-terminal region of SecE (SecE-C) was sufficient for suppression of the secEcs phenotype, confirming the results of Schatz et al. (Schatz, P. J., Bieker, K. L., Ottemann, K. M., Silhavy, T. J., and Beckwith, J. (1991) EMBO J. 10, 1749-1757). SecE-C allowed the overproduction of...

Topics

Adenosine Triphosphate
Bacterial Proteins
Base Sequence
Biological Transport
Blotting, Western
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Escherichia coli Proteins
Membrane Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Plasmids

Protein Biosynthesis

Proteolipids

SEC Translocation Channels

Transcription, Genetic

Source

Open in PubMed

Identifiers

PMID: 1551922

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1551922-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli.PMID 1551922Read ↗

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