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J. Biol. Chem., Vol. 261, Issue 15, 6694-6704, May, 1986
L Pick, H Furneaux and J Hurwitz
The mechanism of action of purified wheat germ RNA ligase has been
examined. ATP was absolutely required for the ligation of substrates
containing 5'-OH or 5'-P and 2',3'-cyclic P or 2'-P termini. Ligation of 1
mol of 5'-P-2',3'-cyclic P-terminated poly(A) was accompanied by the
hydrolysis of 1 mol of ATP to 1 mol each of AMP and PPi. Purified RNA
ligase catalyzed an ATP-PPi exchange reaction, specific for ATP and dATP,
and formed a covalent enzyme-adenylate complex that was detected by
autoradiography following incubation with [alpha-32P]ATP and separation of
the products by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
A protein doublet with a molecular weight of approximately 110 kDa, the
major product detected by silver staining, was labeled in these reactions.
Isolated E-AMP complex was dissociated by the addition of ligatable
poly(A), containing 5'-P-2',3'-cyclic P termini, to yield AMP and by the
addition of PPi to yield ATP. The unique feature of the reactions leading
to an exchange reaction between ATP and PPi and to the formation of an
E-AMP complex was their marked stimulation (up to 400-fold) by the addition
of RNA. This property distinguishes the wheat germ RNA ligase from other
known RNA and DNA ligases which catalyze ATP-PPi exchange reactions and
form E-AMP complexes in the absence of substrate. Thus, RNA appears to
function in two capacities in the wheat germ system: as a cofactor, to
stimulate the reaction of the enzyme with ATP, and as an authentic
substrate for ligation.
Purification of wheat germ RNA ligase. II. Mechanism of action of wheat germ RNA ligase
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