Zur and zinc increase expression of E. coli ribosomal protein L31 through RNA-mediated repression of the repressor L31p

Author:

Rasmussen Rebecca A12,Wang Suning23,Camarillo Jeannie M4,Sosnowski Victoria4,Cho Byoung-Kyu45,Goo Young Ah45,Lucks Julius B1267ORCID,O’Halloran Thomas V2389

Affiliation:

1. Interdisciplinary Biological Sciences Graduate Program, Northwestern University , Evanston , IL 60208, USA

2. Chemistry of Life Process Institute, Northwestern University , Evanston , IL  60208, USA

3. Department of Chemistry, Northwestern University , Evanston , IL  60208, USA

4. Northwestern Proteomics Core, Northwestern University , Evanston , IL  60208, USA

5. Mass Spectrometry Technology Access Center, Washington University in St Louis, School of Medicine , USA

6. Department of Chemical and Biological Engineering, Northwestern University , Evanston , IL 60208, USA

7. Center for Synthetic Biology, Northwestern University , Evanston , IL 60208 , USA

8. Department of Chemistry, Michigan State University , East Lansing , MI 48824 , USA

9. Department of Microbiology & Molecular Genetics, Michigan State University , East Lansing , MI 48824 , USA

Abstract

Abstract Bacteria can adapt in response to numerous stress conditions. One such stress condition is zinc depletion. The zinc-sensing transcription factor Zur regulates the way numerous bacterial species respond to severe changes in zinc availability. Under zinc sufficient conditions, Zn-loaded Zur (Zn2-Zur) is well-known to repress transcription of genes encoding zinc uptake transporters and paralogues of a few ribosomal proteins. Here, we report the discovery and mechanistic basis for the ability of Zur to up-regulate expression of the ribosomal protein L31 in response to zinc in E. coli. Through genetic mutations and reporter gene assays, we find that Zur achieves the up-regulation of L31 through a double repression cascade by which Zur first represses the transcription of L31p, a zinc-lacking paralogue of L31, which in turn represses the translation of L31. Mutational analyses show that translational repression by L31p requires an RNA hairpin structure within the l31 mRNA and involves the N-terminus of the L31p protein. This work uncovers a new genetic network that allows bacteria to respond to host-induced nutrient limiting conditions through a sophisticated ribosomal protein switching mechanism.

Funder

National Science Foundation

National Institutes of Health

Publisher

Oxford University Press (OUP)

Subject

Genetics

Reference70 articles.

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