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

Terminal labeling of embryonic feather keratin mRNA with [3H]KBH4 followed by digestion with ribonuclease T1 and T2, alkaline phosphatase, snake venom phosphodiesterase, and nucleotide pyrophosphatase and analysis of the products by high voltage paper electrophoresis, indicated the presence of the sequence m7G(5')ppp(5')N at the 5'-end of the mRNA. Ribonuclease T1 and A digests of the terminally labeled, and also of unlabeled mRNA followed by fractionation on denaturing polyacrylamide gels indicated the presence of polyadenylate tracts ranging in size from 45 to 165 nucleotide at the 3'-end of the mRNA.
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PMID:The terminal structures of feather keratin mRNA. 49 58

Purified rat liver mitochondria were shown to synthesize poly(adenylic acid) (poly(A)) in vitro. Detection of the poly(A) synthesizing activity was facilitated by addition of NaF to the reaction was shown to be poly(A) by its insensitivity to digestion with pancreatic RNase and RNase T1, its degradation by venom phosphodiesterase and its retention on poly (uridylic acid) 20-23 AMP units and it was covalently attached to the endogenous RNA in the mitochondria. Poly(A) synthesis required ATP and a divalent ion and was maximally active in the pH range of 7-8. The reaction was inhibited by atractyloside, cordycepin triphosphate, Rose Bengal, rifamycin derivative AF/103, sodium pyrophosphate, and N-ethylmaleimide. These studies indicate that the mitochondrial poly(A) polymerase previously described in our laboratory (Jacob, S.T., Rose, K.M., and Morris, H.P. (1974), Biochim. Biophys. Acta 361, 312-320) is involved in the posttranscriptional addition of poly(A) sequence to mitochondrial RNA.
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PMID:Poly(adenylic acid) synthesis in isolated rat liver mitochondria. 99 Feb 63

Solanum nodiflorum mottle virus (SNMV) RNA2 is a single-stranded, covalently closed circular molecule. RNase T2 or nuclease P1 digests of this RNA contain a minor nucleotide of unusual chromatographic and electrophoretic mobility. This nucleotide is resistant to further digestion by T2 or P1 ribonucleases, or by alkali, but is sensitive to venom phosphodiesterase digestion. Alkaline phosphatase digestion yields a product which is RNase T2 and P1 sensitive. The products of these various digests show that the minor nucleotide is a ribonuclease-resistant dinucleotide carrying a 2' phosphomonoester group with the core structure C2'p3'p5'A. This dinucleotide is found in a unique RNase T1 product of SNMV RNA2, thus establishing a unique location in the sequence for the 2' phosphomonoester group at residue 49. Identical results have been obtained with a second related virus. The phosphomonoester group probably results from the RNA ligation event by which the molecules were circularised.
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PMID:2' phosphomonoester, 3'-5' phosphodiester bond at a unique site in a circular viral RNA. 240 85