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)

A complex consisting of the acidic phosphoproteins P0, P1, and P2 (P proteins), L12, and RNA fragments was isolated from rat liver ribosomes after treatment with RNase T1 in the presence of EDTA. The complex was reactive with the anti-28 S RNA antibody specific for the highly conserved "GTPase domain" within 28 S rRNA. This suggests an association of these proteins with the RNA domain. To characterize this complex, the P proteins and L12 were isolated and tested for their binding specificity to the RNA by RNase T1 protection and gel retardation assays. Protein L12 and the P protein complex (P complex) both bound to rat 28 S rRNA and protected sequences comprising residues 1859-1921 and 1838-1936, respectively. The sequences overlap each other and lie in the GTPase domain. An in vitro transcript covering residues 1841-1936 of the 28 S rRNA as well as the protected RNA fragments also showed an ability to bind to the P complex and L12, and the binding was cooperative. RNA sequence elements within residues 1841-1936 required for protein binding were defined using site-directed mutagenesis. A unique internal loop including residues 1858 and 1859 and a distinct subregion comprising residues 1867-1914 in this domain were necessary for the binding of the P complex and L12, respectively. These results indicate that P proteins and L12 bind to restricted sites in the GTPase domain and that the complex constitutes the GTPase-related functional site in mammalian ribosomes.
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PMID:Direct evidence for interaction of the conserved GTPase domain within 28 S RNA with mammalian ribosomal acidic phosphoproteins and L12. 152 39

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