Expression of a cDNA encoding a member of the hexamerin storage proteins from the moth Sesamia nonagrioides (Lef.) during diapause

Spiliotopoulos, Anastasios; Gkouvitsas, Theodoros; Fantinou, Argyro A.; Kourti, Anna

doi:10.1016/j.cbpb.2007.04.014

Cited by 17 publications

(13 citation statements)

References 47 publications

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“…Therefore, one could expect that larvae increase their reserves in preparation for diapause. However, previous reports on insect storage proteins show that not all proteins classified as storage proteins show the same expression trends during diapause [48]–[53]. This heterogeneity of patterns is also reflected in our results.…”

Section: Discussionsupporting

confidence: 71%

Deciphering Proteomic Signatures of Early Diapause in Nasonia

Wolschin

Gadau

2009

PLoS ONE

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Insect diapause is an alternative life-history strategy used to increase longevity and survival in harsh environmental conditions. Even though some aspects of diapause are well investigated, broader scale studies that elucidate the global metabolic adjustments required for this remarkable trait, are rare. In order to better understand the metabolic changes during early insect diapause, we used a shotgun proteomics approach on early diapausing and non-diapausing larvae of the recently sequenced hymenopteran model organism Nasonia vitripennis. Our results deliver insights into the molecular underpinnings of diapause in Nasonia and corroborate previously reported diapause-associated features for invertebrates, such as a diapause-dependent abundance change for heat shock and storage proteins. Furthermore, we observed a diapause-dependent switch in enzymes involved in glycerol synthesis and a vastly changed capacity for protein synthesis and degradation. The abundance of structural proteins and proteins involved in protein synthesis decreased with increasing diapause duration, while the abundance of proteins likely involved in diapause maintenance (e.g. ferritins) increased. Only few potentially diapause-specific proteins were identified suggesting that diapause in Nasonia relies to a large extent on a modulation of pre-existing pathways. Studying a diapause syndrome on a proteomic level rather than isolated pathways or physiological networks, has proven to be an efficient and successful avenue to understand molecular mechanisms involved in diapause.

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Section: Discussionsupporting

confidence: 71%

Deciphering Proteomic Signatures of Early Diapause in Nasonia

Wolschin

Gadau

2009

PLoS ONE

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“…Each band was quantified using the respective Snoβ ‐tubulin band as a reference. We have used β‐tubulin as a control for Real Time and semiquantitative PCR experiments and we have seen that the β‐tubulin mRNA was consistent in different treatments and relative to (1) the nucleic acid concentration (using OD at 260 nm); and (2) the quantity of rRNA bands present in agarose gels (Spyliotopoulos et al. , 2007; Gkouvitsas et al.…”

Section: Methodsmentioning

confidence: 99%

Expression of the Hsp83 gene in response to diapause and thermal stress in the moth Sesamia nonagrioides

Gkouvitsas

Kontogiannatos

Kourti

2009

Insect Molecular Biology

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A full-length Hsp83, named SnoHsp83, cDNA from the corn stalk borer, Sesamia nonagrioides, was cloned and sequenced. Genomic analysis showed that the SnoHsp83 gene is unique. The size of the SnoHsp83 cDNA was found to be approximately 2.6 kb. The deduced polypeptide comprised 717 amino acid residues, with a molecular mass of 82.6 kDa. It contained all the highly conserved amino acid motifs that characterize the cytosolic members of the hsp90 family. We investigated the expression of SnoHsp83 gene in response to diapause and heat/cold stress. SnoHsp83 is constitutively expressed in non-diapausing larvae and is induced 15-fold by heat. SnoHsp83 displays a similar pattern to SnoHsc70 under diapause conditions, when extra larval moults occur. Our results indicate that the SnoHsp83 gene could be involved in the developmental process that occurs between two moults.

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“…The methionine corresponding to translation initiation codon ATG lied at nucleotide positions 27–29, while the translation stop codon TAA was at positions 2 145–2 147. In general, 5′‐untranslated regions of storage protein cDNAs are very short, but 3′‐untranslated regions are quite variable, ranging in size from 80 to 450 nucleotides (Cheon et al ., 2002; Spyliotopoulos et al ., 2007; Tungjitwitayakul et al ., 2008). These two structures of PraAry were in line with these features.…”

Section: Resultsmentioning

confidence: 99%

“…The deduced protein sequence was in accordance with other lepidopteran storage proteins, generally composed of subunits of about 80 kDa (Haunerland, 1996). A signal peptide varying between 15 and 18 aa is a common characteristic among insect storage proteins (Cheon et al ., 2002; Zhu et al ., 2002; Kim et al ., 2003; Ashfaq et al ., 2007; Spyliotopoulos et al ., 2007; Tungjitwitayakul et al ., 2008). Similar to that of other insects, the N‐terminal sequence of PraAry was preceded by a sequence encoding a 16‐aa signal peptide (MKTVLVLASLVALALA), indicating that it was a secreted protein.…”

Section: Resultsmentioning

confidence: 99%

cDNA of an arylphorin‐type storage protein from Pieris rapae with parasitism inducible expression by the endoparasitoid wasp Pteromalus puparum

et al. 2009

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This report presents the cDNA cloning of a storage protein, PraAry, from Pieris rapae and investigates its expression regulated by parasitism of an endoparasitoid wasp Pteromalus puparum. The full‐length cDNA of PraAry is 2 270 nucleotides and contains a 2 121 nucleotide open reading frame encoding 707 amino acids with calculated molecular weights of approximately 83 kDa. Analysis of the primary protein sequence revealed that it possesses a signal peptide of 16 amino acids at the N‐terminus and contains two highly conserved storage protein signature motifs. According to both phylogenetic analysis and the criteria for amino acid composition, PraAry belongs to the subfamily of arylphorin‐type storage protein (1.42% methionine and 18.82% aromatic amino acids). Reverse transcription – polymerase chain reaction analysis indicated that the transcriptional level of PraAry mRNA in P. rapae pupae fat body is inducible in response to parasitism by P. puparum.

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Expression of a cDNA encoding a member of the hexamerin storage proteins from the moth Sesamia nonagrioides (Lef.) during diapause

Cited by 17 publications

References 47 publications

Deciphering Proteomic Signatures of Early Diapause in Nasonia

Deciphering Proteomic Signatures of Early Diapause in Nasonia

Expression of the Hsp83 gene in response to diapause and thermal stress in the moth Sesamia nonagrioides

cDNA of an arylphorin‐type storage protein from Pieris rapae with parasitism inducible expression by the endoparasitoid wasp Pteromalus puparum

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