Nucleic Acids Research, Vol 25, Issue 18 3605-3614, Copyright © 1997 by Oxford University Press
D Esposito and JJ Scocca
The integrases are a diverse family of tyrosine recombinases which
rearrange DNA duplexes by means of conservative site-specific recombination
reactions. Members of this family, of which the well- studied lambda Int
protein is the prototype, were previously found to share four strongly
conserved residues, including an active site tyrosine directly involved in
transesterification. However, few additional sequence similarities were
found in the original group of 27 proteins. We have now identified a total
of 81 members of the integrase family deposited in the databases. Alignment
and comparisons of these sequences combined with an evolutionary analysis
aided in identifying broader sequence similarities and clarifying the
possible functions of these conserved residues. This analysis showed that
members of the family aggregate into subfamilies which are consistent with
their biological roles; these subfamilies have significant levels of
sequence similarity beyond the four residues previously identified. It was
also possible to map the location of conserved residues onto the available
crystal structures; most of the conserved residues cluster in the predicted
active site cleft. In addition, these results offer clues into an apparent
discrepancy between the mechanisms of different subfamilies of integrases.
ARTICLES
The integrase family of tyrosine recombinases: evolution of a conserved active site domain
Laboratory of Molecular Biology, NIDDK, National Institutes of Health, 5 Center Drive MSC0560, Bethesda, MD 20782, USA. domespo@helix.nih.gov
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