Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q8IXL6 (RNS)
 1,091 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Antigen primed macrophage and thymic RNAs hybridize in an antigen restricted fashion. Thymic RNA complementary to the antigen-stimulated macrophage RNA can be obtained from mice inoculated with antigen three days earlier. The ratio of thymic and macrophage RNAs for the optimal hybridization was 50 : 1. The optimal incubation time for hybridization was 32 hours at 60 degrees C. Hybrid RNAs were insensitive to various kinds of RNase. The 31p Fourier transform nuclear magnetic resonance spectra identified hybrid RNA molecules form single stranded RNS's.
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PMID:Antigen restricted hybridization between antigen primed macrophage and thymic RNA. 617 17

An heterologous complex was formed between E. coli protein L1 and P. vulgaris 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 similar to the E. coli 23s RNS region preceding the L1 binding site. The region of mit 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 and the corresponding region of mit 16S rRNA.
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PMID: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. 701 Mar 13

The only RNase genes that have been cloned from higher plants are those expressed in species that are known to exhibit self-incompatibility, such as the S genes of Nicotiana alata. In this report, we investigated whether the expression of this particular type of RNase gene is restricted to self-incompatible species, or if similar genes are expressed in other plants. Using a polymerase chain reaction approach we have identified a set of three putative RNase genes in the self-compatible plant Arabidopsis thaliana (L.) Heynh. ecotype Columbia. These A. thaliana genes, designated RNS1, RNS2, and RNS3, do not cross-hybridize to each other, and their products are homologous to both the S-gene RNases of N. alata and a set of related fungal enzymes. The A. thaliana RNS1, RNS2, and RNS3 genes encode transcripts of 1.1, 1.3, and 1.1 kilobases, respectively, and of the three genes, RNS2 is the most highly expressed in whole plants. The identification of the RNS genes in a self-compatible species suggests that this class of RNases is of general significance in RNA catabolism in higher plants.
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PMID:Genes with Homology to Fungal and S-Gene RNases Are Expressed in Arabidopsis thaliana. 1666 84