The 2′-5′-Oligoadenylate Synthetase 3 Enzyme Potently Synthesizes the 2′-5′-Oligoadenylates Required for RNase L Activation

• Published in: Journal of virology Vol. 88; no. 24; pp. 14222 - 14231
• Main Authors: Ibsen, Mikkel Søes, Gad, Hans Henrik, Thavachelvam, Karthiga, Boesen, Thomas, Desprès, Philippe, Hartmann, Rune
• Format: Journal Article
• Language: English
• Published: United States American Society for Microbiology 01.12.2014
• Subjects: 2',5'-Oligoadenylate Synthetase - metabolism; Adenine Nucleotides - genetics; Adenine Nucleotides - isolation & purification; Adenine Nucleotides - metabolism; Amino Acid Sequence; Baculoviridae - genetics; Baculovirus; Catalytic Domain; Cellular Response to Infection; Endoribonucleases - metabolism; Enzyme Activation; Gene Expression; Genetic Vectors; Humans; Models, Molecular; Molecular Sequence Data; Oligoribonucleotides - genetics; Oligoribonucleotides - isolation & purification; Oligoribonucleotides - metabolism; Protein Conformation; Recombinant Proteins - genetics; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; RNA, Double-Stranded - metabolism; Scattering, Small Angle; Sequence Alignment

The members of the oligoadenylate synthetase (OAS) family of proteins are antiviral restriction factors that target a wide range of RNA and DNA viruses. They function as intracellular double-stranded RNA (dsRNA) sensors that, upon binding to dsRNA, undergo a conformational change and are activated t...