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cDNA of YP4, a follicular epithelium yolk protein subunit, in the moth, Plodia interpunctella
Author(s) -
Perera O.P.,
Shirk Paul D.
Publication year - 1999
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(1999)40:3<157::aid-arch5>3.0.co;2-w
Subject(s) - biology , complementary dna , microbiology and biotechnology , primer (cosmetics) , amino acid , peptide sequence , cdna library , yolk , open reading frame , oocyte , biochemistry , embryo , gene , genetics , ecology , chemistry , organic chemistry
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 . Arch. Insect Biochem. Physiol. 40:157–164, 1999. Published 1999 Wiley‐Liss, Inc. This article is a US Government work and, as such, is in the public domain in the United States of America.