Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.27.3 (RNase T1)
 1,228 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ribosomal protein L11 of Escherichia coli was bound to 23 S rRNA and the resultant complex was digested with ribonuclease T1. A single RNA fragment, protected by protein L11, was isolated from such digests and was shown to rebind specifically to protein L11. The nucleotide sequence of this RNA fragment was examined by two-dimensional fingerprinting of ribonuclease digests. It proved to be 61 residues long and the constituent oligonucleotides could be fitted perfectly between residues 1052 and 1112 of the nucleotide sequence of E. coli 23 S rRNA.
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PMID:The binding site for ribosomal protein L11 within 23 S ribosomal RNA of Escherichia coli. 627 82

The ribosomal protein complex L8 of Escherichia coli consists of two dimers of protein L7/L12 and one monomer of protein L10. This pentameric complex and ribosomal protein L11 bind in mutually cooperative fashion to 23 S rRNA and protect specific fragments of the latter from digestion with ribonuclease T1. Oligonucleotides protected either by the L8 complex alone or by the complex plus protein L11 were isolated from such digests and shown to rebind specifically to these proteins. They were also subjected to nucleotide sequence analysis. The longest oligonucleotide, protected by the L8 complex alone, consisted of residues 1028-1124 of 23 S rRNA and included all the other RNA fragments produced in this study. Previously, protein L11 had been shown to protect residues 1052-1112 of 23 S rRNA. It is concluded that the binding sites for the L8 protein complex and for protein L11 are immediately adjacent within 23 S rRNA of E. coli.
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PMID:The binding site for ribosomal protein complex L8 within 23 s ribosomal RNA of Escherichia coli. 637 61

K+-depleted 60S ribosomal subunits from rat liver were submitted to a mild treatment with ribonuclease T1. Ribonucleoprotein fragments could be separated on sucrose gradients only when the digested subunits were partially deproteinized with a high KCl concentration (0.6 M) which removed seven proteins more or less completely and 5S RNA. The RNA and protein content of each fragment has been characterized. The largest ribonucleoprotein enclosed two RNA fragments of about 950,000 and 750,000 daltons and all the salt-resistant proteins except L5. The smallest one enclosed protein L5 (with L11, L17 and L26 in small amounts) and a 67,000 RNA piece. The subsequent hydrolysis of the large ribonucleoprotein produced several other ribonucleoproteins. One of them has been fully characterized: it enclosed a 250,000 RNA fragment and protein L12 (with L11, L25 and L30 in smaller amounts).
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PMID:Two specific ribonucleoprotein fragments from rat liver 60S ribosomal subunits. 679 92