5′ coding region of the follicular epithelium yolk polypeptide 2 cDNA in the moth,Plodia interpunctella, contains an extended coding region

Shirk, Paul D.; Perera, Omaththage P.

doi:10.1002/(sici)1520-6327(1998)39:3<98::aid-arch2>3.0.co;2-k

Cited by 12 publications

(13 citation statements)

References 27 publications

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“…On the other hand bombycid and pyralid moths retain functional vitellogenin, albeit oogensis and embryogenesis can proceed in its absence (Yamashita and Irie, 1980). The predominant yolk proteins in the absence of vitellogenin are the acid lipase-like proteins, which are synthesised in the ovarian follicle cells and may be involved in mobilisation of lipid from follicle cells to the oocyte during oogenesis (Sato and Yamashita, 1991;Shirk and Perera, 1998).…”

Section: Yolk Proteinsmentioning

confidence: 99%

Comparative and functional genomics of lipases in holometabolous insects

Horne

Haritos

Oakeshott

2009

Insect Biochemistry and Molecular Biology

114

116

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Section: Yolk Proteinsmentioning

confidence: 99%

Comparative and functional genomics of lipases in holometabolous insects

Horne

Haritos

Oakeshott

2009

Insect Biochemistry and Molecular Biology

114

116

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“…The ESP of B. mori (Sato & Yamashita, 1991) and YP2 from P. interpunctella and G. mellonella (Shirk & Perera, 1998) all share similarity with the vertebrate lipoprotein lipases as well as higher Dipteran YPs (Sappington, 2002), and are expressed in the follicular epithelium during the vitellogenic phase of oocyte maturation. In the case of H. cunea , other proteins produced in the follicle cells have been recruited to replace vitellin or have supplanted them as the major yolk proteins.…”

Section: Discussionmentioning

confidence: 98%

“…YP1 and YP2 of H. cunea did not share sequence similarity with any other major yolk proteins such as the lipase‐related proteins ESP from B. mori (Sato & Yamashita, 1991), the FEYP subunit YP2 from P. interpunctella and G. mellonella (Shirk & Perera, 1998) and the YPs of Drosophila melanogaster and other cyclorrhaphan flies (Sappington, 2002), or with the vitellogenins from other insects (Chen et al ., 1997; Sappington & Raikhel, 1998).…”

Section: Discussionmentioning

confidence: 99%

Fat body expressed yolk protein genes in Hyphantria cunea are related to the YP4 follicular epithelium yolk protein subunit gene of pyralid moths

Cheon

Kim

Yun

et al. 2003

Insect Molecular Biology

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cDNA clones for two of the yolk proteins, YP1 and YP2, produced by the fat body of the moth, Hyphantria cunea, were sequenced and found to be homologous to the follicular epithelium yolk proteins of pyralid moths. Both cDNA clones coded for polypeptides of 290 residues and the deduced amino acid sequence identity between YP1 and YP2 was very high (79.0%). Analysis of the secondary structure of the predicted polypeptides suggests that YP1 and YP2 do not form heteromeric proteins because of differences in secondary structure due to the lack of alpha helices in YP1. Northern blot analysis showed that the transcripts for YP1 (1.2 kb) and YP2 (1.1 kb) were present primarily in the female fat body with only trace levels detectable in the ovary of the adult female. In a developmental study, the YP1 and YP2 transcripts were first detectable in 10-day-old pupae and increased into the adult stage. These results suggest that the YP1 and YP2 genes in H. cunea have been recruited to replace the vitellogenin gene as the primary source of yolk proteins. During this process they have acquired a modified pattern of expression that is different from homologous genes reported in pyralid moths. The assessment of the evolution of proteinaceous yolk in these moths should serve as an excellent model for the evolution of gene recruitment.

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“…Our data showed that KK-42BPs from A. prenyi and A. yamamai are likely to be new members of minor yolk proteins, and that both of them contain a lipase-like region. It has been shown that the lepidopetran yolk proteins have sequence similarity with the lipoprotein lipases (Persson et al 1991, Shirk andPerera 1998), however, they are not catalytically active (Pistillo et al 1998, Horne et al 2009). Yolk proteins have been suggested to be ancestors of lipases and are considered ancient animal proteins (Terpstra andGeert 1988, Persson et al 1991).…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Gene Encoding KK-42-Binding Protein in Antheraea pernyi (Lepidoptera: Saturniidae)

Liu

Chen

Qun

et al. 2012

Annals of the Entomological Society of America

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KK-42 is an imidazole insect growth regulator. A (KK-42)-binding protein (KK-42BP) has been shown to be associated with diapause termination in pharate first instars of Antheraea yamamai (Guérin-Méneville) (Lepidoptera: Saturniidae). In this study, the (KK-42)-binding protein gene (ApKK-42BP) was characterized from Antheraea pernyi (Guérin-Méneville) (Lepidoptera: Saturniidae) undergoing a winter diapause as a pupa. Homologous comparison revealed that KK-42BPs from A.pernyi and A.yamamai were closely related to the known minor yolk proteins from the lepidopterans Bombyx mori L., Plodia interpunctella (Hübner), and Galleria mellonella L. The two KK-42BPs also contained a lipase-like region, as observed in the known lepidopteran yolk proteins. Phylogenetic analysis suggested that KK-42BP is a new member of the minor yolk proteins. Reverse transcription-polymerase chain reaction analyses showed that ApKK-42BP mRNA was expressed in all of the tissues tested, throughout four developmental stages, and in both female and male. Both in the brain and hemolymph, expression of ApKK-42BP mRNA level was similar between nondiapause-destined and diapause-destined larval individuals. ApKK-42BP mRNA was expressed in the predia-pause period of diapause-destined pupae, disappeared in early diapause and diapause stage, and reappeared in the postdiapause stage. These expression patterns stated that a lack of KK-42BP is associated with pupal diapause and its expression may be critical to nondiapausing individuals. Our results suggested that the KK-42BP gene is likely involved in a function other than as a yolk protein.

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5′ coding region of the follicular epithelium yolk polypeptide 2 cDNA in the moth,Plodia interpunctella, contains an extended coding region

Cited by 12 publications

References 27 publications

Comparative and functional genomics of lipases in holometabolous insects

Comparative and functional genomics of lipases in holometabolous insects

Fat body expressed yolk protein genes in Hyphantria cunea are related to the YP4 follicular epithelium yolk protein subunit gene of pyralid moths

Characterization of a Gene Encoding KK-42-Binding Protein in Antheraea pernyi (Lepidoptera: Saturniidae)

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