dc.contributor.author |
Gkouvitsas, T |
en |
dc.contributor.author |
Kontogiannatos, D |
en |
dc.contributor.author |
Kourti, A |
en |
dc.date.accessioned |
2014-06-06T06:49:16Z |
|
dc.date.available |
2014-06-06T06:49:16Z |
|
dc.date.issued |
2009 |
en |
dc.identifier.issn |
09621075 |
en |
dc.identifier.uri |
http://dx.doi.org/10.1111/j.1365-2583.2009.00866.x |
en |
dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/4507 |
|
dc.subject |
Diapause |
en |
dc.subject |
Gene expression |
en |
dc.subject |
Heat shock proteins |
en |
dc.subject |
Heat/cold stress |
en |
dc.subject |
Hsc70 |
en |
dc.subject |
Hsp70 |
en |
dc.subject |
Sesamia nonagrioides |
en |
dc.subject.other |
complementary DNA |
en |
dc.subject.other |
heat shock protein 70 |
en |
dc.subject.other |
amino acid sequence |
en |
dc.subject.other |
animal |
en |
dc.subject.other |
article |
en |
dc.subject.other |
chemistry |
en |
dc.subject.other |
cold |
en |
dc.subject.other |
gene expression regulation |
en |
dc.subject.other |
genetics |
en |
dc.subject.other |
growth, development and aging |
en |
dc.subject.other |
heat shock response |
en |
dc.subject.other |
isolation and purification |
en |
dc.subject.other |
larva |
en |
dc.subject.other |
metabolism |
en |
dc.subject.other |
metamorphosis |
en |
dc.subject.other |
molecular genetics |
en |
dc.subject.other |
moth |
en |
dc.subject.other |
nucleotide sequence |
en |
dc.subject.other |
phylogeny |
en |
dc.subject.other |
reverse transcription polymerase chain reaction |
en |
dc.subject.other |
sequence alignment |
en |
dc.subject.other |
sequence homology |
en |
dc.subject.other |
Amino Acid Sequence |
en |
dc.subject.other |
Animals |
en |
dc.subject.other |
Base Sequence |
en |
dc.subject.other |
Cold Temperature |
en |
dc.subject.other |
DNA, Complementary |
en |
dc.subject.other |
Gene Expression Regulation, Developmental |
en |
dc.subject.other |
Heat-Shock Response |
en |
dc.subject.other |
HSP70 Heat-Shock Proteins |
en |
dc.subject.other |
Larva |
en |
dc.subject.other |
Metamorphosis, Biological |
en |
dc.subject.other |
Molecular Sequence Data |
en |
dc.subject.other |
Moths |
en |
dc.subject.other |
Phylogeny |
en |
dc.subject.other |
Reverse Transcriptase Polymerase Chain Reaction |
en |
dc.subject.other |
Sequence Alignment |
en |
dc.subject.other |
Sequence Homology, Amino Acid |
en |
dc.subject.other |
Hexapoda |
en |
dc.subject.other |
Lepidoptera |
en |
dc.subject.other |
Papaipema nebris |
en |
dc.subject.other |
Sesamia nonagrioides |
en |
dc.subject.other |
Zea mays |
en |
dc.title |
Cognate Hsp70 gene is induced during deep larval diapause in the moth Sesamia nonagrioides |
en |
heal.type |
journalArticle |
en |
heal.identifier.primary |
10.1111/j.1365-2583.2009.00866.x |
en |
heal.publicationDate |
2009 |
en |
heal.abstract |
The complete cDNA sequences of Heat shock cognate protein 70 (SnoHsc70) and Heat shock protein 70 (SnoHsp70) were determined from the corn stalk borer Sesamia nonagrioides (Lef.). They encode 653 amino acids (Hsc70) and 633 amino acids (Hsp70), with calculated molecular masses of 71.5 kDa and 70.2 kDa respectively. SnoHsc70 is constitutively expressed, and SnoHsp70 is heat-inducible in non-diapausing insects. SnoHsp70 is down regulated during diapause, while SnoHsc70 is induced as the larvae enter deep diapause. High temperature stress during diapause has no further effect on transcript levels of SnoHsc70. Our results show that SnoHsc70 may play important roles in assisting protein conformation during specific stages of diapause. © 2009 The Royal Entomological Society. |
en |
heal.journalName |
Insect Molecular Biology |
en |
dc.identifier.issue |
2 |
en |
dc.identifier.volume |
18 |
en |
dc.identifier.doi |
10.1111/j.1365-2583.2009.00866.x |
en |
dc.identifier.spage |
253 |
en |
dc.identifier.epage |
264 |
en |