Molecular Biology and Evolution, Vol 14, 829-842, Copyright © 1997 by Society for Molecular Biology and Evolution
KA Balczarek, ZC Lai and S Kumar
The Pax gene family consists of tissue-specific transcriptional regulators
that always contain a highly conserved DNA-binding domain with six
alpha-helices (paired domain), and, in many cases, a complete or residual
homeodomain. Numerous genes of this family have been identified in animals,
with the largest number found in vertebrates. Our evolutionary analyses
indicate that the vertebrate Pax gene family consists of four well-defined
and statistically supported groups: group I (Pax-1, 9), II (Pax-2, 5, 8),
III (Pax-3, 7), and IV (Pax-4, 6). Group I paired domains share a most
recent common ancestor with Drosophila Pox meso, group II with Pox neuro,
group III with paired and gooseberry, and group IV with the eyeless gene.
Two groups containing complete homeodomains (III and IV) are distantly
related, and the intergroup relationships are (I,III), (II,IV). These four
major groups arose before the divergence of Drosophila and vertebrates
prior to the Cambrian radiation of triploblastic metazoan body plans. We
conducted an analysis of fixed radical amino acid differences between
groups in a phylogenetic context. We found that all four fixed radical
amino acid differences between groups I and III are located exclusively in
the N- terminal alpha-helices. Similarly, groups II and IV show three fixed
radical differences in these alpha-helices but at positions different from
those in groups I and III. Implications of such fixed amino acid
differences in potentially generating sequence recognition specificities
are discussed in the context of some recent experimental findings.
ORIGINAL ARTICLE
Evolution of functional diversification of the paired box (Pax) DNA- binding domains
Department of Biology, Pennsylvania State University, University Park 16802, USA.
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