Synthesis of 2-5As possessing base-modified adenosines and their activities to human recombinant RNase L.
The unique 2',5'-oligoadenylate (2-5A) acts as a potent inhibitor of translation in vertebrate cells through the activation of a constituent latent 2-5A-dependent endoribonuclease (RNase L). This 2-5A system plays a major role in the interferon natural defense mechanism against viral infection. We report the syntheses of base-modified adenosine-substituted 2-5A derivatives, their interaction with recombinant human RNase L and their biological stability.
Kitade
Y
Y
Laboratory of Molecular Biochemistry, Department of Biomolecular Science, Faculty of Engineering, Gifu University, Yanagido 1-1, Gifu 501-1193, Japan.
Tanida
Y
Y
Tuboi
T
T
Yoshimura
A
A
Nakanishi
M
M
Yatome
C
C
D000227:Adenine Nucleotides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism*; D000241:Adenosine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D004722:Endoribonucleases / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D015394:Molecular Structure; D009843:Oligoribonucleotides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D013379:Substrate Specificity
D000227:Adenine Nucleotides; D009843:Oligoribonucleotides; D011994:Recombinant Proteins; C023505:2',5'-oligoadenylate; D004722:Endoribonucleases; C031956:2-5A-dependent ribonuclease; D000241:Adenosine