| Literature DB >> 7945354 |
J J Lin1, D L Newton, S M Mikulski, H F Kung, R J Youle, S M Rybak.
Abstract
Onconase, a protein with anti-tumor activity, causes potent inhibition of protein synthesis in the rabbit reticulocyte lysate (IC50 10(-11) M) and when microinjected into Xenopus oocytes (IC50 10(-10) M). Onconase is a member of the RNase A superfamily; however, unlike RNase A, the mechanism of protein synthesis inhibition does not involve apparent degradation of lysate or cellular ribosomal RNAs. Rather, reticulocyte and oocyte tRNA is hydrolyzed after Onconase treatment. Furthermore, re-addition of tRNA to Onconase pretreated lysates or oocytes restores the translational capacity of the system. Taken together these results suggest that Onconase causes potent protein synthesis inhibition by a mechanism involving inactivation of cellular tRNA.Entities:
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Year: 1994 PMID： 7945354 DOI： 10.1006/bbrc.1994.2439
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575