Hirai M, Watanabe D, Kiyota A, Chinzei Y
Department of Medical Zoology, School of Medicine, Mie University, Tsu, Japan.
Insect Biochem Mol Biol. 1998 Aug;28(8):537-47. doi: 10.1016/s0965-1748(98)00052-6.
The bean bug, Riptortus clavatus, has immunologically distinct yolk proteins, vitellin (Vn)-1 and-2 and their precursors, vitellogenin (Vg)-1 and-2. We have cloned the full nucleotide sequence of Vg-1 cDNA. The deduced amino acid sequence has some similarities to other insect Vgs. It contains two polyserine regions, which are characteristic of other Vgs. Vg-1 mRNA appeared after treatment with the juvenile hormone analogue, methoprene, implying transcriptional regulation. We found four enzymatic cleavage sites in the Vg molecule. Two of them match the consensus for dibasic processing endoprotease, which is also conserved in processing sites for other insect Vgs. We showed that the processing at each site was incomplete, and this resulted in production of more than the five polypeptides which would be expected from four processing sites in the molecule. The physiological significance of multiple polypeptides in insect Vgs is still unclear.
