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Updated: Apr 19, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
Published on: September 2, 2019
Multitasking SecB chaperones in bacteria
Ambre Sala1, Patricia Bordes1, Pierre Genevaux1
1Laboratoire de Microbiologie et Génétique Moléculaire, Centre National de la Recherche Scientifique, Université Paul Sabatier, Toulouse, France.
The SecB chaperone aids protein export in bacteria, working with SecA and other chaperones to maintain proteostasis. Its diverse functions extend beyond proteobacteria, impacting various bacterial species and systems.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- The SecB chaperone is crucial for bacterial protein export via the Sec pathway.
- It interacts with the SecA translocase motor for protein targeting to the membrane.
- SecB also plays roles in Sec-independent secretion and general proteostasis.
Purpose of the Study:
- To review the diverse functions of the SecB chaperone.
- To explore SecB's roles beyond canonical protein export in E. coli.
- To highlight SecB-like proteins in other bacteria and their functions.
Main Methods:
- Literature review of SecB chaperone functions.
- Analysis of SecB interactions with other chaperones (trigger factor, DnaK, GroEL).
- Examination of SecB homologs in various bacterial species.
Main Results:
- SecB is essential for Sec-dependent and Sec-independent protein secretion.
- SecB collaborates with other chaperones to regulate proteostasis.
- SecB homologs exhibit diverse roles, including in toxin-antitoxin systems in Mycobacterium tuberculosis.
Conclusions:
- SecB possesses multifaceted roles in bacterial physiology beyond its canonical function.
- The SecB chaperone system is conserved and adapted across diverse bacterial lineages.
- Understanding SecB's varied functions offers insights into bacterial stress response and pathogenesis.
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