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  • Title: The effect of ribosome-inactivating proteins on the ribosome from the hyperthermophilic archaeon Sulfolobus solfataricus.
    Author: Raimo G, Arcucci A, Barbieri L, Valbonesi P, Masullo M, Stirpe F, Bocchini V.
    Journal: Biochem Mol Biol Int; 1998 Apr; 44(4):665-72. PubMed ID: 9584980.
    Abstract:
    Protein synthesis in the thermoacidophilic archaeon Sulfolobus solfataricus (Ss) was inhibited by polynucleotide:adenosine glycosylase activity of some type 1 ribosome-inactivating proteins (RIP). The target of RIP was S. solfataricus rRNA that was depurinated thus producing inactive ribosomes. The amount of RIP required to half-inactivated Ss-ribosomes was comparable to that needed for eubacterial ribosomes, but two orders of magnitude higher than that required for mammalian ribosomes. In addition, RIP treated Ss-ribosomes were also less efficient in stimulating the ribosome dependent GTPase activity of the S. solfataricus elongation factor 2 (SsEF-2) thus suggesting that the inhibition of protein synthesis was probably due to the lack of the interaction between depurinated Ss-ribosomes and SsEF-2. Since SsEF-2 protects Ss-ribosomes against RIP activity it can be hypothesised that also on Ss-ribosomes the sites of interaction for the translocation factor 2 and the RIP are topographically close.
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