Vitellogenin of the cicada Graptopsaltria nigrofuscata (Homoptera): analysis of its primary structure |
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Authors: | Lee J M Nishimori Y Hatakeyama M Bae T W Oishi K |
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Institution: | Graduate School of Science and Technology, Kobe University, Nada, Japan. |
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Abstract: | We cloned and sequenced the cDNA of vitellogenin (Vg) from the cicada Graptopsaltria nigrofuscata (Homoptera). The deduced amino acid sequence of 1987 residues (including 16 residues for a putative signal peptide) was obtained. The pro-Vg was cleaved into two subunits between residues 379 and 380 following a consensus RXXR cleavage site sequence, secreted as S-Vg (apparent molecular weight 43 kDa) and L-Vg (200 kDa), sequestered, and stored in the egg as two vitellins (Vns), S-Vn and L-Vn, with similar respective molecular weights. There was a single long serine-rich stretch closely following the cleavage site. The entire amino acid sequences of the Vgs from the eight insects so far reported could be aligned confidently. The presence of subdomains I-V (areas of relatively high amino acid conservation) and of 10 cysteines at conserved locations at the C-terminus, noted previously among insect Vgs, were confirmed. Antisera raised against G. nigrofuscata S- and L-Vn cross-reacted with the S- and L-Vg/Vn, respectively, of all three other cicada species examined. Another major egg protein (170 kDa) unrelated to Vg/Vn, was also detected in all species examined. |
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