Immunological evidence for the in vivo occurrence of (2'-5')adenylyladenosine oligonucleotides in eukaryotes and prokaryotes.

Laurence, L; Marti, Jacques; Roux, Damien; Cailla, H.

doi:10.1073/pnas.81.8.2322

Cited by 34 publications

(21 citation statements)

References 35 publications

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“…The findings reported here demonstrate conclusively the occurrence of 7-5' oligoadenylates in the prokaryote E. coli and confirm our preliminary observations [2]. The earlier experiments were done with bacteria grown in nutrient broth and led to the demonstration of the occurrence of the dimer, trimer and tetramer 5'OH 2'-5' oligoadenylates.…”

Section: Discussionsupporting

confidence: 79%

The occurrence of 2'-5' oligoadenylates in Escherichia coli

et al. 1987

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The use of a highly specific radioimmunoassay and of HPLC permitted us to confirm the occurrence of 2′–5′ oligoadenylates [px(A2′p5′)nA] in several strains of Escherichia coli. Cellular concentrations of 2′–5′ oligoadenylates ranged from 50 nM to 300 nM. The mixture of 2′–5′ oligoadenylates consisted primarily of pppA2′p5′A, pA2′p5′A, A2′p5′Ap and A2′p5′A under normal conditions of growth. None of them activated R Nase L. Infection of the bacteria with the single‐stranded DNA phage M13 or induction of a heat‐inducible, non‐lytic mutant of phage λ led to a significant increase in the total pool of 2′–5′ oligoadenylates, paralleling the progressive inhibition of growth. Likewise, the inhibition of protein synthesis with chloramphenicol stimulated the accumulation of 2′–5′ oligoadenylates. Furthermore, the inhibition of bacterial growth by either phage or by chloramphenicol brought about a change in the composition of the 2′–5′ oligoadenylate pool; 5′‐phosphorylated 2′–5′ oligoadenylates accumulated and became the major components. The findings indicate a parallelism between the effects of viral infection on the synthesis of 2′–5′ oligoadenylates in eukaryotes and similar effects subsequent to phage growth in the bacterium E. coli.

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Section: Discussionsupporting

confidence: 79%

The occurrence of 2'-5' oligoadenylates in Escherichia coli

et al. 1987

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“…Furthermore, a dominant negative mutant of endoribonuclease suppresses the anti-EMCV antiviral effect of interferon . Other reports have demonstrated the presence of 2-5A oligomers in different tissues of mouse and significantly enhanced levels during virus infection (Laurence et al, 1984;. Besides a possible role in mediating resistance to virus infection, the 2-A system has also been implicated in the control of cell growth and differentiation (Williams and Sil-verman, 1985;Hassel et al, 1993;Rysiecki et al, 1989;Kimchi et al, 1981aKimchi et al, , 1981bFerbus et al, 1985;Krause et al, 1985).…”

mentioning

confidence: 99%

69‐kDa and 100‐kDa Isoforms of Interferon‐Induced (2′‐5′)Oligoadenylate Synthetase Exhibit Differential Catalytic Parameters

Marié

Blanco

Rebouillat

et al. 1997

European Journal of Biochemistry

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The (2'-S')oligoadenylate synthetase represents a family of interferon-induced proteins which when activated by double-stranded (ds)RNA polymerizes ATP into 2'-S'-linked oligomers with the general formula pppA(2'pS'A),, where n > 1, which for convenience are referred to as 2-5A. We studied here the influence of pH, dsRNA concentration and time on oligomeric composition of 2-5A synthesized by purified 69-kDa and 100-kDa isoforms of (2'-S')oligo(adenylate) synthetase. In optimal conditions for activity, the 69-kDa forin synthesized higher oligomers of 2-5A molecules whereas the 100 kDa form synthesized preferentially dinieric molecules, which are known not to be functional for the activation of RNase L. This difference does not reflect a differential affinity of the enzymes for the preformed 2-SA dimer, which is found to be a very poor substrate for both enzymes. This latter strongly suggests that the mechanism of elongation is more likely processive. Moreover, we show that both isoforms have efficient nucleotidyl-transferase activity and provide evidence that, in optimized conditions, GTP can be used alone as substrate by these enzymes to generate pppG2'pS'G. Our results clearly demonstrate that the 69-kDa and 100-kDa forms of (2'-5')oligoadenylate synthetase manifest various differential catalytic activities, and favor the hypothesis that these enzymes might have other functions in the cell besides those in the 2-5A system.

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“…A partial loss of the antiviral effects of IFN was seen in cells deficient in the (2'-5') oligo A synthetase (Salzberg et al, 1983), deficient in the (2'-5') oligo A-activated RNase F (Epstein et al, 1981) or when this RNase was inhibited by (2'-5')A analogs (Watling et al, 1985) although this is probably not the only mechanism by which IFN inhibits virus growth (Lebleu and Content, 1982). The (2'-5') oligo A nucleotides have been detected in many eukaryotic cells and even in bacteria (Laurence et al, 1984) and 2'-specific synthetase may be widespread. The mammalian IFN-induced enzyme has been purified from mouse (Dougherty et al, 1980) and human cells (Yang et al, 1981;Revel et al, 1981); a large and a small form of the enzyme have been observed St.…”

Section: Introductionmentioning

confidence: 99%

Structure of two forms of the interferon-induced (2′-5′) oligo A synthetase of human cells based on cDNAs and gene sequences.

Benech¹,

Mory²,

Revel³

et al. 1985

The EMBO Journal

192

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The (2′‐5′) oligo A synthetase E, one of the translational inhibitory enzymes whose synthesis is strongly induced by all interferons (IFNs), is shown to be encoded in human cells by a 13.5‐kb gene. By a cell‐specific differential splicing, between the seventh and an additional eighth exon of this gene, two active E mRNAs of 1.6 and 1.8 kb are produced, along with several longer transcripts. cDNA clones for the two mRNAs were obtained and their sequences indicate that the human (2′‐5′) oligo A synthetase gene codes for two forms of the enzyme of mol. wt. 41 000 and 46 000, which differ only by their C‐terminal ends. The product of the 1.6‐kb RNA (E16) has a very hydrophobic C terminus, which is replaced by a longer acidic C‐terminal sequence in the 1.8‐kb RNA product (E18). The transcriptional start site of the gene was identified and 200 bp of the 5′ flanking region were sequenced. A strong homology was found between this region of the IFN‐activated (2′‐5′) oligo A synthetase gene and the corresponding region of the human fibroblast IFN‐beta 1 gene, whose transcription is also stimulated by IFN priming. The gene has two polyadenylation sites which share a common undecanucleotide, but are used in a cell‐specific manner to give rise to the 1.6‐ and 1.8‐kb mRNAs.

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Immunological evidence for the in vivo occurrence of (2'-5')adenylyladenosine oligonucleotides in eukaryotes and prokaryotes.

Cited by 34 publications

References 35 publications

The occurrence of 2'-5' oligoadenylates in Escherichia coli

The occurrence of 2'-5' oligoadenylates in Escherichia coli

69‐kDa and 100‐kDa Isoforms of Interferon‐Induced (2′‐5′)Oligoadenylate Synthetase Exhibit Differential Catalytic Parameters

Structure of two forms of the interferon-induced (2′-5′) oligo A synthetase of human cells based on cDNAs and gene sequences.

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