B. Mentrup et W. Weidemann, The exon-intron organization of the prohormone convertase PC2 gene from the insect Lucilia cuprina, GENE, 237(1), 1999, pp. 29-33
Prohormone or proprotein convertases are members of the subtilisin family o
f serine proteases. They are involved in the activation of precursor molecu
les by endoproteolytic cleavage at basic amino acid residues. Among the dif
ferent members of this prohormone convertase family, the prohormone convert
ase 2 (PC2) is almost exclusively expressed in endocrine and neuroendocrine
tissues and plays an important role in the endoproteolytic processing of p
rohormones.
Here we describe the exon-intron organization of the PC2 gene from the inse
ct Lucilia cuprina by characterization of PCR-amplified genomic DNA fragmen
ts. The insect PC2 gene contains 12 exons with an estimated size of over 14
.5 kb.
The exon sizes range from 38 bp to >448 bp. All identified intron-exon boun
daries are consistent with the GT-AG-rule.
A comparison of the genomic structures of the thus far known prohormone con
vertase genes with that of the insect PC2 gene revealed a conservation of t
he positions of most introns interrupting the exons coding for the amino-te
rminal and catalytic domains. This conservation is consistent with the sugg
estion of a common evolutionary origin for the prohormone convertase gene f
amily. (C) 1999 Elsevier Science B.V. All rights reserved.