| RNA 3'-terminal phosphate cyclase | <enzyme> ATP dependent; forms 2',3' terminal cyclic phosphate on RNA which is then the substrate for RNA ligase of hela cells Registry number: EC 6.5.- Synonym: RNA tph cyclase (26 Jun 1999) |
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| RNA, antisense | An RNA molecule which, by binding to a complementary sequence in either RNA or DNA, inhibits the function and/or completion of synthesis of the latter molecule. It is involved in various regulatory systems in vivo. Artificial antisense rnas have been used to inhibit translation of specific mRNA molecules both in living cells (eukaryotic and bacterial) and in cell-free systems. (12 Dec 1998) |
| RNA, archaeal | Ribonucleic acid in archaea having regulatory and catalytic roles as well as involvement in protein synthesis. (12 Dec 1998) |
| RNA, bacterial | Ribonucleic acid in bacteria having regulatory and catalytic roles as well as involvement in protein synthesis. (12 Dec 1998) |
| RNA-binding proteins | Proteins which bind to RNA molecules. Certain structure motifs are common to several of the proteins, such as arginine (arg)-rich tracts, typically consisting of alternating arg-asp, arg-ser, or arg-gly residues. These proteins also tend to have a common ribonucleotide sequence domain. (12 Dec 1998) |
| RNA cap analogs | Analogs of RNA cap compounds which do not have a positive charge. These compounds inhibit the initiation of translation of both capped and uncapped messenger RNA. (12 Dec 1998) |
| RNA caps | Compounds with the general structure 7-methyl-5'-guanosine triphosphate-5'-x which modify the 5' end of eukaryotic cellular and viral messenger RNA and some heterogeneous nuclear rnas. These compounds, which are positively charged, protect the above specified rnas at their termini against attack by phosphatases and other nucleases and promote mRNA function at the level of initiation of translation. Analogs of the RNA caps (RNA cap analogs), which lack the positive charge, inhibit the initiation of protein synthesis. (12 Dec 1998) |
| RNA, catalytic | RNA which contains an intron sequence that has an enzyme-like catalytic activity. This intron sequence has been shown to fold up to form a complex surface that can function like an enzyme in reactions with other RNA molecules and thus synthesise new molecules even in the absence of protein. (12 Dec 1998) |
| RNA, chloroplast | Ribonucleic acid in chloroplasts having regulatory and catalytic roles as well as involvement in protein synthesis. (12 Dec 1998) |
| RNA, complementary | Synthetic transcripts of a specific DNA molecule or fragment, made by an in vitro transcription system. This crna can be labelled with radioactive uracil and then used as a probe. (12 Dec 1998) |
| RNA-dependent ATPase | <enzyme> Requires single-stranded polynucleotide as cofactor Registry number: EC 3.6.1.- Synonym: atpase, RNA-dependent (26 Jun 1999) |
| RNA-directed DNA polymerase | <enzyme> An enzyme that synthesises DNA on an RNA template. It is encoded by the pol gene of retroviruses and by certain retrovirus-like elements. Chemical name: Deoxynucleotide-triphosphate:DNA deoxynucleotidyltransferase (RNA-directed) Registry number: EC 2.7.7.49 (12 Dec 1998) |
| RNA, double-stranded | RNA consisting of two strands as opposed to the more prevalent single-stranded RNA. most of the double-stranded segments are formed from transcription of DNA by intramolecular base-pairing of inverted complementary sequences separated by a single-stranded loop. Some double-stranded segments of RNA are normal in all organisms. (12 Dec 1998) |
| RNA editing | <molecular biology> Specific alterations of RNAs, for example C_V changes that are not coded for in the genes. (23 Aug 1998) |
| RNA enzyme | <molecular biology> Often referred to as RNA with catalytic capacity, an enzyme made of nucleic acid not protein that catalyse chemical reactions, often the breakdown of other RNAs. Of particular interest because of the implications for self replicating systems in the earliest stages of the evolution of (terrestrial) life. Their discovery in the mid-1980s refuted the concept that only proteins could be biological catalysts. There is potential for their use as pharmaceuticals and industrial catalysts. (13 Nov 1997) |