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The effect of ribosome‐inactivating proteins on the ribosome from the hyperthermophilic archaeon Sulfolobus solfataricus
Author(s) -
Raimo Gennaro,
Arcucci Alessandro,
Masullo Mariorosario,
Bocchini Vincenzo,
Barbieri Luigi,
Valbonesi Paola,
Stirpe Fiorenzo
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800201712
Subject(s) - sulfolobus solfataricus , ribosome , elongation factor , protein biosynthesis , biology , biochemistry , translation (biology) , ribosomal protein , rna , archaea , messenger rna , gene
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.