An interferon-induced phosphodiesterase degrading (2'-5') oligoisoadenylate and the C-C-A terminus of tRNA. | Zendy

A. Schmidt | Zendy; Yuti Chernajovsky | Zendy; Lester M. Shulman | Zendy; P. Federman | Zendy; Hanna Berissi | Zendy; Michel Revel | Zendy

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An interferon-induced phosphodiesterase degrading (2'-5') oligoisoadenylate and the C-C-A terminus of tRNA.

Author(s) -

A. Schmidt,

Yuti Chernajovsky,

Lester M. Shulman,

P. Federman,

Hanna Berissi,

Michel Revel

Publication year - 1979

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.76.10.4788

Subject(s) - phosphodiester bond , phosphodiesterase , ribonuclease , biochemistry , interferon , transfer rna , enzyme , activator (genetics) , oligonucleotide , chemistry , microbiology and biotechnology , amino acid , biology , rna , gene , virology

A phosphodiesterase characterized by a generally higher activity on 2'-5' than on 3'-5' phosphodiester bonds was isolated from mouse L cells treated with interferon. A similar enzyme was purified from mouse reticulocytes. The phosphodiesterase 2'-PDi splits the 2'-phosphate bond of pppA2'p5'A2'p5'A, the oligonucleotide activator of ribonuclease F. The level of phosphodiesterase 2'-PDi is increased by interferon treatment of L cells. The phosphodiesterase was also shown to degrade the C-C-A terminus of tRNA and to reduce the amino acid acceptance of tRNA in cell-free extracts, thereby causing a tRNA-reversible inhibition of mRNA translation.

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