Related Experiment Video
Updated: Mar 15, 2026

Measuring Peptide Translocation into Large Unilamellar Vesicles
Published on: January 27, 2012
An antimicrobial origin of transit peptides accounts for early endosymbiotic events
1CNRS/UPMC, Institut de Biologie Physico-Chimique, Paris, France.
Abstract:
Primary endosymbiosis, which gave rise to mitochondria or chloroplasts, required successful targeting of a number of proteins from the host cytosol to the endosymbiotic organelles. A survey of studies published in separate fields of biological research over the past 40 years argues for an antimicrobial origin of targeting peptides. It is proposed that mitochondria and chloroplast derive from microbes that developed a resistance strategy to antimicrobial peptides that consisted in their rapid internalization and proteolytic disposal by microbial peptidases.
More Related Videos
Related Concept Videos
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Protein Transport into the Inner Mitochondrial Membrane
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Transduction
Eukaryotic Evolution
Contrary to the endosymbiont theory, the eukaryote-first hypothesis proposes that the simpler prokaryotic and...
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.
Protein Transport to the Inner Chloroplast Membrane

