scholarly journals The respective roles of the protein kinase and pppA2′ p5′ A2′ p5′ A-activated endonuclease in the inhibition of protein synthesis by double stranded RNA in rabbit reticulocyte lysates

1979 ◽  
Vol 6 (4) ◽  
pp. 1335-1350 ◽  
Author(s):  
Bryan R.G. Williams ◽  
Christopher S. Gilbert ◽  
Ian M. Kerr
Keyword(s):  
Protein Synthesis ◽  
Protein Kinase ◽  
Double Stranded Rna ◽  
Inhibition Of Protein Synthesis ◽  
Reticulocyte Lysates

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

2005 ◽  
Vol 187 (9) ◽  
pp. 3151-3157 ◽  
Author(s):  
Ana J. Muñoz-Gómez ◽  
Marc Lemonnier ◽  
Sandra Santos-Sierra ◽  
Alfredo Berzal-Herranz ◽  
Ramón Díaz-Orejas
Keyword(s):  
Protein Synthesis ◽  
Dna Replication ◽  
Rna Degradation ◽  
Double Stranded Rna ◽  
Cellular Processes ◽  
Inhibition Of Protein Synthesis ◽  
Reticulocyte Lysates ◽  
The Stability ◽  
Cole1 Replication

ABSTRACT 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.

Reversal of the double-stranded-RNA-induced inhibition of protein synthesis by a catalytically inactive mutant of the protein kinase PKR

1993 ◽  
Vol 214 (3) ◽  
pp. 945-948 ◽  
Author(s):  
Tyson V. SHARP ◽  
Qiurong XIAO ◽  
Ian JEFFREY ◽  
Dirk R. GEWERT ◽  
Michael J. CLEMENS
Keyword(s):  
Protein Synthesis ◽  
Protein Kinase ◽  
Double Stranded Rna ◽  
Inhibition Of Protein Synthesis
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