Nucleic Acids Research, 1992, Vol. 20, No. 8 1959-1965
© 1992
MOLECULAR BIOLOGY |
The major RNA in prosomes*of HeLa cells and duck erythroblasts is tRNALys3

Institut Jacques Monod du CNRS, Université Paris 7, 2 place Jussieu 75251 Paris Cedex 05 1Institut de Biologie Moléculaire et Cellulaire du CNRS and Centre de Recherches de Biologie Moléculaire et Cellulaire de ||'Université Louis Pasteur 15 rue René Descartes, 67084 Strasbourg Cedex, France
+To whom correspondence should be addressed
Received December 31, 1991. Revised March 8, 1992. Accepted March 8, 1992.
Two-dimensional gel electrophoresis of HeLa cell prosomal RNAs, 3'-end labeled by RNA ligase, revealed one prominent spot. Determination of a partial sequence at the 3'-end Indicated full homology to the 18 nucleotides at the 3-end of tRNALys3 from rabbit, the bovine and the human species. An oligonucleotide complementary to the 3'-end of tRNALys3 hybridized on Northern blots with prosomal RNA from both HeLa cells and duck erythroblasts. In two-dimensional PAGE, the major pRNA of HeLa cells co-migrated with bovine tRNALys3. Reconstitution of the CCA 3'-end of RNA from both human and duck prosomes, by tRNA-nucleotidyl-transferase, confirmed the tRNA character of this type of RNA. Furthermore, it revealed at least one additional tRNA band about 85 nt long among the prosomal RNA from both species. Finally, confirming an original property of prosomal RNA, we show that in vitro synthesized tRNALys3 hybridizes stably to duck globin mRNA, and to poly(A)+- and poly(A)-RNA from HeLa cells.
*The term Prosome introduced by our laboratory (1) for the then unknown particle is used here and, speaking of its protease activity, the term Multicatalytic Proteinase or MCP following the recommendation of the group of the enzymologists concerned (Dahlman et al. (2), Oriowski and Wilk (3)), in preference to the term Proteasome suggested by Arrigo et al(4).
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