| Autor: |
Joshi, Avatar, Mahmoud, Samar A., Kim, Soo-Kyoung, Ogdahl, Justyne L., Lee, Vincent T., Chien, Peter, Yildiz, Fitnat H. |
| Předmět: |
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| Zdroj: |
PLoS Genetics; 6/26/2020, Vol. 16 Issue 6, p1-24, 24p |
| Abstrakt: |
The LonA (or Lon) protease is a central post-translational regulator in diverse bacterial species. In Vibrio cholerae, LonA regulates a broad range of behaviors including cell division, biofilm formation, flagellar motility, c-di-GMP levels, the type VI secretion system (T6SS), virulence gene expression, and host colonization. Despite LonA's role in cellular processes critical for V. cholerae's aquatic and infectious life cycles, relatively few LonA substrates have been identified. LonA protease substrates were therefore identified through comparison of the proteomes of wild-type and ΔlonA strains following translational inhibition. The most significantly enriched LonA-dependent protein was TfoY, a known regulator of motility and the T6SS in V. cholerae. Experiments showed that TfoY was required for LonA-mediated repression of motility and T6SS-dependent killing. In addition, TfoY was stabilized under high c-di-GMP conditions and biochemical analysis determined direct binding of c-di-GMP to LonA results in inhibition of its protease activity. The work presented here adds to the list of LonA substrates, identifies LonA as a c-di-GMP receptor, demonstrates that c-di-GMP regulates LonA activity and TfoY protein stability, and helps elucidate the mechanisms by which LonA controls important V. cholerae behaviors. Author summary: This study provides insights into the mechanisms and consequences of LonA-mediated regulated proteolysis in Vibrio cholerae, the causal organism of the acute diarrheal disease cholera that is endemic in more than 47 countries across the globe. Lon is broadly conserved in bacterial systems; uncovering the molecular connection between c-di-GMP signaling and LonA-mediated proteolysis of V. cholerae will provide conceptual frameworks for the development of intervention strategies to combat virulence by bacterial pathogens. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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