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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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- 한국잠사학회 International Journal of Industrial Entomology International Journal of Industrial Entomology 제28권 제2호
- 발행연도
- 2014.1
- 수록면
- 71 - 84 (14page)
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The full-length heat shock protein 88 (HSP88) complementary DNA (cDNA) of Paecilomycestenuipes Jocheon -1 was obtained by screening the Paecilomyces tenuipes (P. tenuipes) Jocheon-1 Uni-Zap cDNA library and performing 5' RACE polymerase chain reaction(PCR). The P. tenuipes Jocheon-1 HSP88 cDNA contained an open reading frame (ORF) of2,139-basepair encoding 713 amino acid residues. The deduced amino acid sequence of theP. tenuipe s Jocheon-1 HSP88 cDNA showed 77% identity to Nectria haematococca HSP88and 45-76% identity to other fungal homologous HSP88s. Phylogenetic analysis and BLASTprogram analysis confirmed that the deduced amino acid sequences of the P. tenuipesJocheon-1 HSP88 gene belonged to the ascomycetes group within the fungal clade. The P.
tenuipes Jocheon-1 HSP88 also contained the conserved ATPase domain at the N-terminalregion. The cDNA encoding P. tenuipes Jocheon-1 HSP88 was expressed as an 88 kilodalton(kDa) polypeptide in baculovirus-infected insect Sf9 cells. Under higher temperature conditionsfor the growth of the entomopathogenic fungus, mRNA expression of P. tenuipes Jocheon-1HSP88 was quantified by real time PCR (qPCR). The results showed that heat shock stressinduced a higher level of mRNA expression compared to normal growth conditions.
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참고문헌 (24)
참고문헌 신청
Bendz H / 2007 / Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling
Benjamin IJ / 1998 / Stress (heat shock) proteins:molecular chaperones in cardiovascular biology and disease / Circ. Res 83 : 117 ~ 132
Binder RJ / 2008 / Heat-shock protein-based vaccines for cancer and infectious disease / Expert. Rev. Vaccines 7 (3) : 383 ~ 393
Bork P / 1992 / An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin and Hsp70 heat shock proteins / Proc Natl Acad Sci USA 89 : 7290 ~ 7294
Buchberger A / 1994 / The chaperone function of DNA K requires the coupling of ATPase activity with substrate binding through residue E171 / EMBO J 13 : 1687 ~ 1695
Benjamin IJ / 1998 / Stress (heat shock) proteins:molecular chaperones in cardiovascular biology and disease / Circ. Res 83 : 117 ~ 132
Binder RJ / 2008 / Heat-shock protein-based vaccines for cancer and infectious disease / Expert. Rev. Vaccines 7 (3) : 383 ~ 393
Bork P / 1992 / An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin and Hsp70 heat shock proteins / Proc Natl Acad Sci USA 89 : 7290 ~ 7294
Buchberger A / 1994 / The chaperone function of DNA K requires the coupling of ATPase activity with substrate binding through residue E171 / EMBO J 13 : 1687 ~ 1695
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