FEBS Letters | |
2′‐Adenylated derivatives of Ap3A activate RNase L | |
Justesen, Just1  Turpaev, Kyril1  Hartmann, Rune1  | |
[1] Department of Molecular and Structural Biology, Aarhus University, Mollers Alle 130, Aarhus 8000, Denmark | |
关键词: RNase L; 2-5A synthetase; Ap3A; (2′-5′)oligoadenylate; Interferon; Oligoadenylate synthesis; Poly(I)·poly(C); AC50; half-maximal activating concentration; Ap3A; diadenosine triphosphate; 2-5A; (2′-5′)oligoadenylate; BAP; bovine alkaline phosphatase; FPLC; fast protein liquid chromatography; IFN; interferon; TCA; trichloroacetic acid; WRS; tryptophanyl-tRNA synthetase; | |
DOI : 10.1016/S0014-5793(99)00996-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The exact physiological function of Ap3A (A5′ppp5″A, 5′5″ diadenosine triphosphate) remains unclear. Previously we have demonstrated that the human p46 2-5A synthetase (OAS1) efficiently utilises Ap3A as an acceptor substrate for oligoadenylate synthesis. Here we show that Ap3A(2′p5′A) n oligonucleotides can activate the 2-5A-dependent RNase (RNase L), when the number of 2′,5′-linked adenyl residues is two or more. Under the experimental conditions applied the half-maximal activation (AC50) of RNase L for 2′-adenylated Ap3A derivatives was determined to be in nanomolar range while the AC50 for 2-5A3 was 0.4 nM. The Ap3A(2′p5′A) n oligonucleotides are thus less effective in activating RNase L than 2-5A. We also investigated the occurrence of 2′-adenylated Ap3A in interferon and poly(I)·poly(C)-treated HeLa cells. In purified trichloroacetic acid-soluble extracts about 40% of RNase L-activating material is resistant to phosphatase treatment, whereas the removal of 5′-terminal phosphates greatly reduces the activating properties of 2-5A. We assume that this activity at least partly may be associated with the presence of 2′-adenylated Ap n A derivatives with blocked 5′-terminal phosphates.
【 授权许可】
Unknown
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