Molecular Biology and Evolution, Vol 4, 364-379, Copyright © 1987 by Society for Molecular Biology and Evolution
PE Gibbs and A Dugaiczyk
We have recently determined complete DNA sequences for the human albumin
and alpha-fetoprotein [AFP] genes and thus have identified their detailed
structures. Each is composed of three domains of four exons, three of which
are internal and one of which is a domain-linking exon. Equivalent exons in
each domain show sufficient sequence and structural similarity to be
considered homologous; additional unique exons at each end of the gene show
no similarity to the internal triplicated structures. Since earlier,
conflicting evolutionary models were based on analysis of single gene
structures, we derived from five genes a series of consensus sequences
representing the three internal exons as well as the domain-linking exon.
The five genes were human and rat albumin and human, mouse, and rat AFP
genes. Structurally equivalent exons of the different domains are shown to
have arisen from a single exon in a one-domain precursor. Exons that bridge
the domains arose from an unequal crossover that fused two exons of the
precursor. Our model suggests that part of the coding sequence of the
one-domain precursor may have been derived from an intron, by way of loss
of a splice site. The consensus sequences were used to propose an intron-
exon structure for the related gene encoding the serum vitamin D- binding
protein (DBP). DBP is truncated relative to albumin and AFP, and we submit
that this results from deletion of two internal exons in the third domain
of the gene rather than from premature termination of the coding sequence.
ORIGINAL ARTICLE
Origin of structural domains of the serum-albumin gene family and a predicted structure of the gene for vitamin D-binding protein
Department of Biochemistry, University of California, Riverside 92521.
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