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Updated: Jul 6, 2026

Quantifying Yersinia pseudotuberculosis Type III Secretion System Activity Following Iron Starvation and Anaerobic Growth
Published on: May 31, 2024
RNase E regulates the Yersinia type 3 secretion system
Jing Yang1, Chaitanya Jain, Kurt Schesser
1University of Miami, Miller School of Medicine, Department of Microbiology and Immunology, Miami, FL 33136, USA.
Abstract:
Yersinia spp. use a type 3 secretion system (T3SS) to directly inject six proteins into macrophages, and any impairment of this process results in a profound reduction in virulence. We previously showed that the exoribonuclease polynucleotide phosphorylase (PNPase) was required for optimal T3SS functioning in Yersinia pseudotuberculosis and Yersinia pestis. Here we report that Y. pseudotuberculosis cells with reduced RNase E activity are likewise impaired in T3SS functioning and that phenotypically they resemble Delta pnp cells. RNase E does not affect expression levels of the T3SS substrates but instead, like PNPase, regulates a terminal event in the secretion pathway. This similarity, together with the fact that RNase E and PNPase can be readily copurified from Y. pseudotuberculosis cell extracts, suggests that these two RNases regulate T3SS activity through a common mechanism. This is the first report that RNase E activity impacts the T3SS as well as playing a more general role in infectivity.
Insights
RNase E, like polynucleotide phosphorylase (PNPase), is crucial for the type 3 secretion system (T3SS) in Yersinia. Both enzymes regulate a late stage in the secretion pathway, impacting bacterial virulence.
Area of Science:
- Microbiology
- Molecular Biology
- Bacterial Pathogenesis
Background:
- Yersinia spp. utilize a type 3 secretion system (T3SS) to inject effector proteins into host macrophages, which is essential for virulence.
- Polynucleotide phosphorylase (PNPase) was previously identified as a key regulator of T3SS function in Yersinia species.
Purpose of the Study:
- To investigate the role of RNase E in the T3SS functioning of Yersinia pseudotuberculosis.
- To elucidate the relationship between RNase E, PNPase, and T3SS regulation.
Main Methods:
- Phenotypic analysis of Y. pseudotuberculosis with reduced RNase E activity.
- Assessing T3SS substrate expression levels.
- Copurification of RNase E and PNPase from bacterial cell extracts.
Main Results:
- Reduced RNase E activity in Y. pseudotuberculosis impairs T3SS function, phenotypically similar to PNPase-deficient mutants.
- RNase E does not alter T3SS substrate expression but regulates a terminal secretion step.
- RNase E and PNPase can be copurified, indicating a potential shared regulatory mechanism.
Conclusions:
- RNase E is a novel regulator of the Yersinia T3SS, acting through a mechanism similar to PNPase.
- These findings suggest a common pathway involving RNase E and PNPase in controlling T3SS activity and bacterial infectivity.
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