Ej. Higgins et al., THE ATP ANALOG CONTAINING A METHYLENE GROUP IN-PLACE OF THE 5'-OXYGENSERVES AS A SUBSTRATE FOR BACTERIOPHAGE-T3 RNA-POLYMERASE, Nucleosides & nucleotides, 14(8), 1995, pp. 1671-1674
Transcription reactions catalyzed by bacteriophage T3 RNA polymerase a
nd using CTP, GTP, UTP and an analogue of ATP containing a methylene g
roup in place of the 5' oxygen yield RNA-like polymers. These products
are degraded to the 5'-mononucleotides CMP, GMP, UMP, and the corresp
onding analogue of AMP by exposure to snake venom phosphodiesterase. B
y using appropriate DNA templates, a single residue of the AMP analogu
e can be located at the site adjacent to the cleavage position in the
substrate strand of a hammerhead ribozyme. The modified substrate stra
nd is completely resistant to cleavage by the ribozyme's catalytic str
and.