The 5' region of YP2 cDNA, a follicular epithelium yolk protein subunit in the moth, Plodia interpunctella, shows that the polypeptide contains an extended internal coding region. Partial cDNA clones for YP2 were isolated from a pharate adult female ovarian cDNA expression library in Lambda Zap II b
cDNA of YP4, a follicular epithelium yolk protein subunit, in the moth, Plodia interpunctella
✍ Scribed by O.P. Perera; Paul D. Shirk
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 205 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0739-4462
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✦ Synopsis
YP4, a subunit of the follicular epithelium yolk protein in the moth, Plodia interpunctella, is produced in the follicle cells during vitellogenesis and after secretion is taken up into the oocyte and stored in the yolk spheres for utilization during embryogenesis. In order to identify the cDNA clones for YP4, a degenerate PCR primer was designed to six amino acid residues identified in the NH 2 -terminal sequence of mature YP4. The YP4 degenerate primer plus T7 reverse PCR primer produced a PCR product from a cDNA library for the majority of the YP4 coding sequence. Combined cDNA and 5¢ RACE sequencing showed the YP4 transcript to be 991 bp in length with a single open reading frame for a predicted polypeptide of 299 amino acids. Northern analysis showed a single YP4 transcript was present in ovarian RNA that was approximately 1 kb in length. The predicted amino acid sequence for YP4 from P. interpunctella was most closely related to the predicted YP4 protein from the moth, Galleria mellonella, and the spherulin 2a protein from the slime mold, Physarum polycephalum.
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