RNase/Anti-RNase Activities of the Bacterial parD Toxin-Antitoxin System
| Autor: | Sandra Santos-Sierra, Ramón Díaz-Orejas, Alfredo Berzal-Herranz, Ana J. Muñoz-Gómez, Marc Lemonnier |
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| Rok vydání: | 2005 |
| Předmět: |
DNA Replication
RNase P Endoribonuclease Bacterial Toxins Molecular Sequence Data education Mutation Missense Genetics and Molecular Biology Biology Microbiology chemistry.chemical_compound Ribonucleases Bacterial Proteins Protein biosynthesis Escherichia coli Animals Molecular Biology Protein Synthesis Inhibitors Base Sequence Cell-Free System Escherichia coli Proteins DNA replication RNA Toxin-antitoxin system Molecular biology humanities DNA-Binding Proteins chemistry Amino Acid Substitution Rabbits Antitoxin human activities DNA Plasmids |
| Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname |
| Popis: | The bacterial parD toxin-antitoxin system of plasmid R1 encodes two proteins, the Kid toxin and its cognate antitoxin, Kis. Kid cleaves RNA and inhibits protein synthesis and cell growth in Escherichia coli. Here, we show that Kid promotes RNA degradation and inhibition of protein synthesis in rabbit reticulocyte lysates. These new activities of the Kid toxin were counteracted by the Kis antitoxin and were not displayed by the KidR85W variant, which is nontoxic in E. coli. Moreover, while Kid cleaved single- and double-stranded RNA with a preference for UAA or UAC triplets, KidR85W maintained this sequence preference but hardly cleaved double-stranded RNA. Kid was formerly shown to inhibit DNA replication of the ColE1 plasmid. Here we provide in vitro evidence that Kid cleaves the ColE1 RNA II primer, which is required for the initiation of ColE1 replication. In contrast, KidR85W did not affect the stability of RNA II, nor did it inhibit the in vitro replication of ColE1. Thus, the endoribonuclease and the cytotoxic and DNA replication-inhibitory activities of Kid seem tightly correlated. We propose that the spectrum of action of this toxin extends beyond the sole inhibition of protein synthesis to control a broad range of RNA-regulated cellular processes. This work was supported by grants from the Spanish Ministerio de Ciencia y Tecnología (SAF-2002-04649), the CSIC (PIES 200420E006 and 200420E062), and the Spanish REIPI Network of the “Fondo de Investigaciones Sanitarias” (CO314). |
| Databáze: | OpenAIRE |
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