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RNase/Anti-RNase Activities of the Bacterial parD Toxin-Antitoxin System

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dc.creator Muñoz-Gómez, Ana J.
dc.creator Lemonnier, Marc
dc.creator Santos-Sierra, Sandra
dc.creator Berzal-Herranz, Alfredo
dc.creator Díaz-Orejas, Ramón
dc.date 2008-04-03T09:24:06Z
dc.date 2008-04-03T09:24:06Z
dc.date 2005-05
dc.date.accessioned 2017-01-31T01:01:27Z
dc.date.available 2017-01-31T01:01:27Z
dc.identifier J Bacteriol. 2005 May; 187(9): 3151–3157
dc.identifier 1098-5530
dc.identifier http://hdl.handle.net/10261/3432
dc.identifier 10.1128/JB.187.9.3151-3157.2005
dc.identifier.uri http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3432
dc.description 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.
dc.description 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).
dc.description Peer reviewed
dc.format 214537 bytes
dc.format application/pdf
dc.language eng
dc.publisher American Society for Microbiology
dc.rights openAccess
dc.title RNase/Anti-RNase Activities of the Bacterial parD Toxin-Antitoxin System
dc.type Artículo


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