THE SECONDARY STRUCTURE OF THE PROTEIN L1 BINDING REGION OF RIBOSOMAL 23S RNA - HOMOLOGIES WITH PUTATIVE SECONDARY STRUCTURES OF THE L11 MESSENGER-RNA AND OF A REGION OF MITOCHONDRIAL 16S-RRNA
THE SECONDARY STRUCTURE OF THE PROTEIN L1 BINDING REGION OF RIBOSOMAL 23S RNA - HOMOLOGIES WITH PUTATIVE SECONDARY STRUCTURES OF THE L11 MESSENGER-RNA AND OF A REGION OF MITOCHONDRIAL 16S-RRNA
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DOI:
10.1093/nar/9.2.293
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发表时间:
1981-01-01
影响因子:
14.9
通讯作者:
EBEL, JP
中科院分区:
文献类型:
--
作者:
BRANLANT, C;KROL, A;EBEL, JP
An heterologous complex was formed betweenE. coliprotein L1 andP. vulgavis23S 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 andNaja oxiananuclease digestions respectively. By comparison of these results with those previously obtained with the homologous regions ofE. coliandB. stearothermophilus23S RNAs, we postulate a general structure for the protein L1 binding region of bacterial 23S RNA. Both mouse and human mit 16S rRNAs andXenopus laevisandTetrahymena28S rRNAs contain a sequence similarto theE. coli23S 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.