Related Experiment Video
Updated: Jul 18, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Chloroplast SecA and Escherichia coli SecA have distinct lipid and signal peptide preferences
Changqi Sun1, Sharyn L Rusch, Jinoh Kim
1Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269-3125, USA.
Abstract:
Like prokaryotic Sec-dependent protein transport, chloroplasts utilize SecA. However, we observe distinctive requirements for the stimulation of chloroplast SecA ATPase activity; it is optimally stimulated in the presence of galactolipid and only a small fraction of anionic lipid and by Sec-dependent thylakoid signal peptides but not Escherichia coli signal peptides.
Related Concept Videos
Protein Transport to the Thylakoids
Protein Transport to the Outer Chloroplast Membrane
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Biosynthesis of Lipids
Insertion of Single-pass Transmembrane Proteins in the RER
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Protein Transport to the Inner Chloroplast Membrane
Signal Sequences and Sorting Receptors

