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J. Biol. Chem., Vol. 259, Issue 22, 14255-14264, 11, 1984
CS Craik, QL Choo, GH Swift, C Quinto, RJ MacDonald and WJ Rutter
A family of approximately 10 trypsin genes was detected in a rat genomic
library by hybridization and in vivo recombination techniques using cloned
rat pancreatic trypsin I and II cDNAs as probes. Two separate clones
containing the entire trypsin I gene and most of the trypsin II gene were
sequenced. Four introns split the trypsin I coding sequence. The positions
of the first three introns of the trypsin II gene are identical with those
in the trypsin I gene (the fourth intron was not present in the trypsin II
clone). The coding regions of the two genes are 88% homologous; the
5'-noncoding regions are 92% homologous, whereas the 3'-noncoding regions
share 66% identity. In contrast, the proximal 5'-flanking regions from -1
to -500 which may contain the elements controlling gene expression are less
than 30% conserved overall, but segments of approximately 70% homology can
be discerned in this region. Some of these sequences are homologous to
sequences found in the chymotrypsin and elastase genes. More distal
upstream sequences (-500 to -2500) and the intervening sequences show no
evident sequence homology (less than 20%). Unique sequences containing
homopolymeric purine/pyrimidine repeats are found 2.5 kilobases upstream
from the start of transcription of the trypsin I gene and within the second
and third introns of the trypsin II gene. The nucleotide homologies as well
as the similarities of intron positions of the two trypsin genes to those
of other serine protease genes clearly support an evolutionary relationship
between members of this gene family.
Structure of two related rat pancreatic trypsin genes
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