Nucleic Acids Research, Vol 25, Issue 3 648-653, Copyright © 1997 by Oxford University Press
AS Sjogren, E Pettersson, BM Sjoberg and R Stromberg
The catalytic mechanism for self-splicing of the group I intron in the
pre-mRNA from the nrdB gene in bacteriophage T4 has been investigated using
2'-amino- 2'-deoxyguanosine or guanosine as cosubstrates in the presence of
Mg2+, Mn2+and Zn2+. The results show that a divalent metal ion interacts
with the cosubstrate and thereby influences the efficiency of catalysis in
the first step of splicing. This suggests the existence of a metal ion that
catalyses the nucleophilic attack of the cosubstrate. Of particular
significance is that the transesterification reactions of the first step of
splicing with 2'- amino-2'-deoxyguanosine as cosubstrate are more efficient
in mixtures containing either Mn2+or Zn2+together with Mg2+than with only
magnesium ions present. The experiments in metal ion mixtures show that two
(or more) metal ions are crucial for the self-splicing of group I introns
and suggest the possibility that more than one of these have a direct
catalytic role. A working model for a two-metal-ion mechanism in the
transesterification steps is suggested.
ARTICLES
Metal ion interaction with cosubstrate in self-splicing of group I introns
Department of Molecular Biology, Arrhenius Laboratory, Stockholm University, S-10691 Stockholm, Sweden.
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