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JBC, Vol. 252, Issue 5, 1732-1738, Mar, 1977
A. Sugino, T. J. Snoper and N. R. Cozzarelli
Bacteriophage T4 RNA ligase catalyzes the ATP-dependent ligation of a
5'-phosphoryl-terminated nucleic acid donor to a 3'-hydroxyl-terminated
nucleic acid acceptor. We have identified adenylylated DNA and RNA reaction
intermediates in which the AMP moiety is attached by a pyrophosphate bond
to the 5'-phosphoryl group of the donor. A large amount of DNA-adenylate
accumulates during the reaction and the dependence of joining and
adenylylation on chain length are similar. The adenylylated donor is joined
by ligase to an acceptor in the absence of ATP, and AMP is released
stoichiometrically in this reaction. The acceptor is not only a substrate
in the reaction but also a cofactor for adenylylation of the donor; in the
absence of a 3'-hydroxyl group the activated intermediate does not form.
The activated DNA need not join to the acceptor that initially stimulated
activation but can also join to another acceptor. This process of acceptor
exchanges has proven useful for promoting the cyclization of small DNA
substrates and the synthesis of DNA co-polymers.
Bacteriophage T4 RNA ligase. Reaction intermediates and interaction of substrates
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