R. Tatsumi et al., 2 ',5 '-oligoadenylate synthetase gene in chicken: gene structure, distribution of alleles and their expression, BBA-GENE ST, 1494(3), 2000, pp. 263-268
Citations number
36
Categorie Soggetti
Molecular Biology & Genetics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION
We have cloned the gene for chicken 2',5'-oligoadenylate synthetase (ChOAS)
by the method of polymerase chain reaction with use of ChOAS cDNA sequence
. The ChOAS gene is composed of five introns and six exons containing all o
f the sequence of the ChOAS cDNA from the start to the stop codon. The firs
t five exons of ChOAS gene which encode the OAS catalytic domain have a sim
ilar structure to HuOAS1 gene including the exon-intron boundaries. However
, the length of introns of ChOAS gene is only 1/7 of those of HuOAS1 gene.
The sixth exon of the ChOAS gene encodes the ubiquitin-like (UbL) domain of
two consecutive sequence (UbL1 and UbL2) homologous to ubiquitin. ChOAS en
coded in a single copy gene has at least two alleles, OAS*A and OAS*B. The
differences between these two alleles are in the sixth exon of the gene; a
96-nucleotide sequence in the UbL1 portion of OAS*A is deleted from OAS*B.
No OAS*B gene was detected in nine lines of chickens tested other than Legh
orns. Almost the same levels of ChOAS-A and -B proteins induced physiologic
ally in erythrocytes were detected in infant chickens (2-week-old), but in
grown-up chickens (6-month-old) the level of erythrocyte OAS-B was markedly
reduced in most of BIB chickens. Thus, the UbL domain of ChOAS is responsi
ble for the maintenance of the OAS level in the tissue. (C) 2000 Elsevier S
cience B.V. All rights reserved.