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Translation/secretion coupling by type III secretion systems.

J E Karlinsey¹, J Lonner, K L Brown

¹Department of Microbiology, University of Washington, Seattle 98195, USA.

|August 31, 2000

Summary

Type III secretion chaperones regulate protein translation and secretion. The chaperone FIgN controls translation of the flgM gene, impacting bacterial virulence protein export.

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Area of Science:

Microbiology
Molecular Biology
Bacterial Pathogenesis

Background:

Type III secretion systems (T3SS) are crucial for exporting virulence factors and flagellar components in Gram-negative bacteria.
T3SS chaperones are known to prevent substrate degradation, but their role in translation is less understood.

Purpose of the Study:

To investigate the role of T3SS chaperones in regulating the translation of secreted proteins.
To determine if chaperones influence the fate of secreted proteins based on their mRNA transcript.

Main Methods:

Analyzing the effect of the chaperone FIgN on the translation of the flgM gene from different mRNA transcripts.
Comparing the cellular localization (secretion vs. cytoplasmic retention) of FIgM produced from distinct transcripts.

Main Results:

FIgN is essential for flgM gene translation from a flagellar class 3 transcript but not a class 2 transcript.
FIgM translated from the class 3 transcript is secreted, while FIgM from the class 2 transcript remains cytoplasmic.
Evidence suggests both mRNA and amino acid sequences act as secretion signals for T3SS substrates.

Conclusions:

Type III secretion chaperones have a novel role in coupling protein translation with secretion.
Bacterial secretion substrates may possess dual mRNA and amino acid secretion signals.
This finding expands the known functions of T3SS chaperones beyond substrate protection.