Characterization of the cDNA encoding the 90 kDa heat-shock protein in the Lepidoptera Bombyx mori and Spodoptera frugiperda

Landais, Igor; Pommet, Jean-Michel; Mita, Kasuei; Nohata, Junko; Gimenez, Sylvie; Fournier, Philippe; Devauchelle, G.; Duonor-Cérutti, Martine; Ogliastro, Mylène

doi:10.1016/s0378-1119(01)00523-6

Cited by 56 publications

(53 citation statements)

References 29 publications

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“…Many other interesting genes have been identified in SilkBase, which have provided tools for homology-based identification of related genes in other insects, as well as phylogenetic analysis. These genes include a bacteria-induced serine proteinase inhibitor serpin found in Manduca sexta (40), heat shock protein and related genes in Spodoptera frugiperda (41,42), and a member of the cadherin superfamily associated with resistance to the Bacillus thuringiensis ␦-endotoxin Cry1Ac in Heliothis virescens (43).…”

Section: Overview Of Resultsmentioning

confidence: 99%

The construction of an EST database for Bombyx mori and its application

Mita

Morimyo

Okano

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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249

213

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Section: Overview Of Resultsmentioning

confidence: 99%

The construction of an EST database for Bombyx mori and its application

Mita

Morimyo

Okano

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

249

213

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“…Hence, the HSP90 family provides a useful model system for evolutionary studies (Gupta 1995). In addition, the response of these proteins to environmental stresses, such as changes in temperature (Palmisano et al 2000;Hermesz et al 2001;Landais et al 2001), hyperosmotic shock (Pan et al 2000), hypoxia (Li et al 2008), metal ions (Ali et al 1996), polychlorinated biphenyls (Wiens et al 2000), and also diseases (Ramaglia et al 2004) has been examined. Despite of these various studies, only five complete cDNA sequences have been reported from mollusks (Farcy et al 2007;Gunter and Degnan 2007), including three HSP90 cDNA sequences in bivalves (Gao et al 2007(Gao et al , 2008Choi et al 2008).…”

Section: Discussionmentioning

confidence: 99%

Molecular characterization and induction of heat shock protein 90 in the Antarctic bivalve Laternula elliptica

Kim

Ahn

Kim

et al. 2009

Cell Stress and Chaperones

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Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that plays a key role in protein synthesis, folding, denaturation prevention, and signal transduction. We cloned the complete complementary DNA (cDNA) sequence of the Laternula elliptica HSP90. The full-length cDNA was 2,823 bp in size and contained an open reading frame of 2,190 bp that was translated into 729 amino acids with a calculated molecular weight of 83.4 kDa. The deduced amino acid sequence of HSP90 showed the highest homology to Haliotis tuberculata HSP90 (83%). Reverse-transcriptase polymerase chain reaction analysis revealed the presence of HSP90 transcripts in all of the tissues examined. We also studied the transcriptional expression pattern of HSP90 exposed to thermal stress with real-time polymerase chain reaction. The relative expression level of HSP90 messenger RNA was upregulated and peaked at 12 h in the digestive gland and at 24 h in the gills, then dropped progressively.

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“…This intron regulates the basal transcription of the cytoplasmic hsp90 at normal physiological temperatures (Lange et al, 1997). However, this intron is missing in the cytoplasmic hsp90 of Lepidoptera (Landais et al, 2001;Sonoda et al, 2006).…”

Section: Specificity Of Lepidoptera Hsp90 Gene and Universal Primersmentioning

confidence: 99%

“…Lepidopteran cytoplasmic hsp90 is a single-copy gene without introns (Landais et al, 2001;Sonoda et al, 2006). After aligning existing sequences of cytoplasmic HSP90, a highly conserved region was located in the 3' untranslated region (UTR) in Lepidoptera, which is not present in the alignments of Diptera and Hymenoptera (data not shown).…”

Section: Introductionmentioning

confidence: 99%

Universal primers for amplifying the complete coding sequence of cytoplasmic heat shock protein 90 (HSP90) in Lepidoptera

Xu¹,

Li²,

Xiao³

et al. 2011

Eur. J. Entomol.

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Abstract. Using sequence alignment, a conserved domain in the 3' untranslated region (UTR) of the cytoplasmic heat shock protein 90 (HSP90) of Lepidoptera was found. This region is highly variable in other insect groups. Furthermore, universal primers were designed to amplify the complete coding sequence (CDS) of HSP90 from total genomic DNA in Lepidoptera, avoiding the commonly used reverse transcription-polymerase chain reaction (RT-PCR) and 3', 5'-rapid amplification of cDNA ends (RACE) methods based on cDNA. These primers amplified a fragment of about 2.25 kb in the 11 species tested, which represent seven different families of Lepidoptera, including moths and butterflies. The results suggest that the conserved domain of 3'UTR is universal in Lepidoptera and these primers successfully amplify the complete CDS of cytoplasmic HSP90 from genomic DNA.

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Characterization of the cDNA encoding the 90 kDa heat-shock protein in the Lepidoptera Bombyx mori and Spodoptera frugiperda

Cited by 56 publications

References 29 publications

The construction of an EST database for Bombyx mori and its application

The construction of an EST database for Bombyx mori and its application

Molecular characterization and induction of heat shock protein 90 in the Antarctic bivalve Laternula elliptica

Universal primers for amplifying the complete coding sequence of cytoplasmic heat shock protein 90 (HSP90) in Lepidoptera

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