Synthesis of Adenylyl-(3', 5')-Nucleosides, Adenylyl-(3', 5')-Guanosine 2',3'-Cyclic Phosphate, and Oligoadenylic Acids by Ribonuclease U2

Koike, Tatsuro; Uchida, Tsuneko; Egami, Fujio

doi:10.1093/oxfordjournals.jbchem.a129439

Cited by 8 publications

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“…RNase T2 cleaves all RNA residues but prefers A residue46. RNase U2 specifically cleaves unpaired A residue47. RNase H cleaves DNA/RNA duplex to produce ssDNA via hydrolytic mechanism4849.…”

Section: Discussionmentioning

confidence: 99%

Identification of an RNase that preferentially cleaves A/G nucleotides

Xie

Chen

Zhang

et al. 2017

Sci Rep

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Ribonucleases play an important role in the RNA metabolism which is critical for the localization, stability and function of mature RNA transcripts. More and more ribonucleases were discovered in recent years with the progress of technology. In the present study, we found that the uncharacterized C19orf43, a novel interacting protein of human telomerase RNA (hTR), digested T7 transcribed RNA, total cellular RNA and RNA oligos but not DNA. Thus we named this new RNase as hTRIR (human telomerase RNA interacting RNase). Genetic analysis showed that hTRIR is conserved among eukaryotic species and widely expressed in different cell lines. The RNase activity of hTRIR works in a broad temperature and pH range while divalent cations are not required. The conserved C-terminus of C19orf43 is necessary for its activity. Finally, we found that hTRIR cleaves all four unpaired RNA nucleotides from 5′ end or 3′ end with higher efficiency for purine bases, which suggested that hTRIR is an exoribonuclease. Taken together, our study showed the first evidence of the novel function of hTRIR in vitro, which provides clue to study the regulatory mechanism of hTR homeostasis in vivo.

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Section: Discussionmentioning

confidence: 99%

Identification of an RNase that preferentially cleaves A/G nucleotides

Xie

Chen

Zhang

et al. 2017

Sci Rep

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Large scale synthesis of dinucleoside monophosphates catalyzed by ribonuclease from Aspergillus clavatus

Bauer

Lamed

Lapidot

1972

Biotech & Bioengineering

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A gram scale enzymatic synthesis of eight dinucleoside monophosphates (ApC, ApU, CpC, CpU, GpC, GpU, UpC, and UpU) is described. The synthesis involves a reaction between the appropriate ribonucleoside-2',3'-cyclic phosphates and cytidine or uridine in the presence of ribonuclease from Aspergillus clavatus at 30°C. The enzyme is removed from the reaction mixture by chromatography on Bio-Gel P4, and the dinucleoside monophosphate is further purified by chromatography on a DEAF,-Sephadex A-25, column.A procedure for the large scale preparation of the ribonuclease from Aspergillus clavatus is also described.

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Ribonuclease U2

Schomburg¹,

Salzmann²

1991

Enzyme Handbook 3

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Synthesis of Adenylyl-(3', 5')-Nucleosides, Adenylyl-(3', 5')-Guanosine 2',3'-Cyclic Phosphate, and Oligoadenylic Acids by Ribonuclease U2

Cited by 8 publications

References 0 publications

Identification of an RNase that preferentially cleaves A/G nucleotides

Identification of an RNase that preferentially cleaves A/G nucleotides

Large scale synthesis of dinucleoside monophosphates catalyzed by ribonuclease from Aspergillus clavatus

Ribonuclease U2

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