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Article

Bacterial Sec protein transport is rate-limited by precursor length: a single turnover study.

Molecular biology of the cell - 1 Oct 2009

Liang Fu-Cheng, Bageshwar Umesh K, Musser Siegfried M

Abstract excerpt

An in vitro real-time single turnover assay for the Escherichia coli Sec transport system was developed based on fluorescence dequenching. This assay corrects for the fluorescence quenching that occurs when fluorescent precursor proteins are transported into the lumen of inverted membrane vesicles. We found that 1) the kinetics were well fit by a single exponential, even when the ATP concentration was...

Topics

Adenosine Triphosphatases
Adenosine Triphosphate
Adenylyl Imidodiphosphate
Bacterial Outer Membrane Proteins
Bacterial Proteins
Dose-Response Relationship, Drug
Escherichia coli
Escherichia coli Proteins
Kinetics
Membrane Transport Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Nickel

Protein Precursors

Protein Transport

SEC Translocation Channels

SecA Proteins

Spectrometry, Fluorescence

Succinic Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 19656854
DOI: 10.1091/mbc.e09-01-0075
PMCID: PMC2754939

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