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Nucleic Acids Research, 1981, Vol. 9, No. 2 293-307
© 1981


MOLECULAR BIOLOGY

The secondary structure of the protein L1 binding region of ribosomal 23S RNA. Homologies with putative secondary structures of the L11 mRNA and of a region of mitochondrial 16S rRNA

Christiane Branlant*, Alain Krol, Ali Machatt and Jean-Pierre Ebel

Institut de Biologie Moléculaire et Cellulaire du C.N.R.S., Université Louis Pasteur de Strasbourg 15, rue René Descartes, 67084 Strasbourg Cedex, France

To wohm correspondence should be sent

Received November 6, 1980. An heterologous complex was formed between E. coli protein L1 and P. vulgavis 23S RNA. We determined the primary structure of the RNA region which remained associated with protein L1 after RNase digestion of this complex. We also identified the loci of this RNA region which are highly susceptible to T1, S1 and Naja oxiana nuclease digestions respectively. By comparison of these results with those previously obtained with the homologous regions of E. coli and B. stearothermophilus 23S RNAs, we postulate a general structure for the protein L1 binding region of bacterial 23S RNA. Both mouse and human mit 16S rRNAs and Xenopus laevis and Tetrahymena 28S rRNAs contain a sequence similarto the E. coli 23S rRNA region preceding the L1 binding site. The region ofmit 16S rRNA which follows this sequence has a potential secondary structure bearing common features with the L1-associated region of bacterial 23S rRNA. The 5'- end region of the L11 mRNA also has several sequence potential secondary structures displaying striking homologies with the protein L1 binding region of 23S rRNA and this probably explains how protein L1 functions as a translational repressor. One of the L11 mRNA putative structures bears the features common to both the L1-associated region of bacterial 23S rRNA andthe corresponding region of mit 16S rRNA.


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