Related Experiment Video
Updated: Dec 24, 2025

Modifying Baculovirus Expression Vectors to Produce Secreted Plant Proteins in Insect Cells
Published on: August 20, 2018
The Evolution of Protein Secretion Systems by Co-option and Tinkering of Cellular Machineries
Rémi Denise1, Sophie S Abby2, Eduardo P C Rocha3
1Microbial Evolutionary Genomics, Institut Pasteur, CNRS, UMR3525, Paris, 75015, France; Sorbonne Université, Collège Doctoral, F-75005 Paris, France.
Abstract:
Protein secretion is important for many biotic and abiotic interactions. The evolution of protein secretion systems of bacteria, and related nanomachines, occurred by the co-option of machineries for motility, conjugation, injection, or adhesion. Some of these secretion systems emerged many times, whereas others are unique. In most cases, their evolution occurred by successive rounds of gene accretion, deletion, and horizontal transfer, resulting in machines that can be very different from the original ones. The frequency with which such co-option processes occurred seems to depend on the complexity of the systems, their differences to the ancestral machines, the availability of genetic material to tinker with, and possibly on the mechanisms of effector recognition. Understanding the evolution of secretion systems illuminates their functional diversification and could drive the discovery of novel systems.
Related Concept Videos
Bacterial Translocation and Protein Secretion
Gram-negative Bacterial Protein Secretion Systems
Overview of Secretory Vesicles
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
Protein Translocation Machinery on the ER Membrane
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
Post-translational Translocation of Proteins to the RER
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...

