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Article

SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.

The Journal of biological chemistry - 15 May 1990

Akita M, Sasaki S, Matsuyama S, Mizushima S

Abstract excerpt

SecA is an acidic, peripheral membrane protein involved in the translocation of secretory proteins across the cytoplasmic membrane. The direct interaction of SecA with secretory proteins was demonstrated by means of chemical cross-linking with 1-ethyl-3-(3-dimethylaminoprophyl)carbodiimide. OmpF-Lpp, a model secretory protein, carries either an uncleavable or cleavable signal peptide, and mutant secretory...

Topics

Bacterial Outer Membrane Proteins
Bacterial Proteins
Base Sequence
Biological Transport
Cell Membrane
Cross-Linking Reagents
Electrochemistry
Escherichia coli
Ethyldimethylaminopropyl Carbodiimide
Isoelectric Point

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Protein Precursors

Protein Sorting Signals

Source

Identifiers

PMID: 2159471

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2159471-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.PMID 2159471Read ↗

In vitro kinetic analysis of the role of the positive charge at the amino-terminal region of signal peptides in translocation of secretory protein across the cytoplasmic membrane in Escherichia coli.Semantic proximity Read ↗

SecY-SecY and SecY-SecG contacts revealed by site-specific crosslinking.Semantic proximity Read ↗

Defining the role of the Escherichia coli chaperone SecB using comparative proteomics.Semantic proximity Read ↗

Covalently dimerized SecA is functional in protein translocation.Semantic proximity Read ↗

Export of beta-lactamase is independent of the signal recognition particle.Semantic proximity Read ↗

SecA protein: autoregulated initiator of secretory precursor protein translocation across the E. coli plasma membrane.Semantic proximity Read ↗

Preprotein transfer to the Escherichia coli translocase requires the co-operative binding of SecB and the signal sequence to SecA.Semantic proximity Read ↗

SecA is required for the insertion of inner membrane proteins targeted by the Escherichia coli signal recognition particle.Semantic proximity Read ↗

Dimeric SecA is essential for protein translocation.Semantic proximity Read ↗

SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein.Semantic proximity Read ↗

Membrane deinsertion of SecA underlying proton motive force-dependent stimulation of protein translocation.Semantic proximity Read ↗

Bacterial protein translocation requires only one copy of the SecY complex in vivo.Semantic proximity Read ↗

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