Molecular Characterization of Heat-Induced HSP11.0 and Master-Regulator HSF from Cotesia chilonis and Their Consistent Response to Heat Stress

Small heat shock proteins (sHSPs) are members of the heat shock protein (HSP) family that play an important role in temperature stress, and heat shock factors (HSFs) are transcriptional activators that regulate HSP expression. Cotesia chilonis, the major endoparasitoid of Chilo suppressalis, modulates the C. suppressalis population in the field. In this study, we cloned and characterized two genes from C.chilonis: the heat-induced HSP11.0 gene (Cchsp11.0) that consisted of a 306-bp ORF, and the master regulator HSF (Cchsf) containing an 1875-bp ORF. CcHSP11.0 contained a chaperonin cpn10 signature motif that is conserved in other hymenopteran insects. CcHSF is a typical HSF and contains a DNA-binding domain, two hydrophobic heptad repeat domains, and a C-terminal trans-activation domain. Neither Cchsp11.0 or Cchsf contain introns. Real-time quantitative PCR revealed that Cchsp11.0 and Cchsf were highly induced at 36 °C and 6 °C after a 2-h exposure. Overall, the induction of Cchsf was lower than Cchsp11.0 at low temperatures, whereas the opposite was true at high temperatures. In conclusion, both Cchsp11.0 and Cchsf are sensitive to high and low temperature stress, and the expression pattern of the two genes were positively correlated during temperature stress.

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Heat shock factor 2 is required for maintaining proteostasis against febrile-range thermal stress and polyglutamine aggregation

Molecular Biology of the Cell ◽

10.1091/mbc.e11-04-0330 ◽

2011 ◽

Vol 22 (19) ◽

pp. 3571-3583 ◽

Cited By ~ 37

Author(s):

Toyohide Shinkawa ◽

Ke Tan ◽

Mitsuaki Fujimoto ◽

Naoki Hayashida ◽

Kaoru Yamamoto ◽

...

Keyword(s):

Thermal Stress ◽

Heat Shock ◽

Protein Misfolding ◽

Reproductive Organs ◽

Heat Shock Factors ◽

Mild Heat ◽

Promising Therapeutic Target ◽

Αb Crystallin ◽

Shock Proteins ◽

Polyglutamine Protein

Heat shock response is characterized by the induction of heat shock proteins (HSPs), which facilitate protein folding, and non-HSP proteins with diverse functions, including protein degradation, and is regulated by heat shock factors (HSFs). HSF1 is a master regulator of HSP expression during heat shock in mammals, as is HSF3 in avians. HSF2 plays roles in development of the brain and reproductive organs. However, the fundamental roles of HSF2 in vertebrate cells have not been identified. Here we find that vertebrate HSF2 is activated during heat shock in the physiological range. HSF2 deficiency reduces threshold for chicken HSF3 or mouse HSF1 activation, resulting in increased HSP expression during mild heat shock. HSF2-null cells are more sensitive to sustained mild heat shock than wild-type cells, associated with the accumulation of ubiquitylated misfolded proteins. Furthermore, loss of HSF2 function increases the accumulation of aggregated polyglutamine protein and shortens the lifespan of R6/2 Huntington's disease mice, partly through αB-crystallin expression. These results identify HSF2 as a major regulator of proteostasis capacity against febrile-range thermal stress and suggest that HSF2 could be a promising therapeutic target for protein-misfolding diseases.

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Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability.

Genes & Development ◽

10.1101/gad.5.10.1902 ◽

1991 ◽

Vol 5 (10) ◽

pp. 1902-1911 ◽

Cited By ~ 234

Author(s):

K D Sarge ◽

V Zimarino ◽

K Holm ◽

C Wu ◽

R I Morimoto

Keyword(s):

Heat Shock ◽

Dna Binding ◽

Heat Shock Factors ◽

Binding Ability

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Characterization of progesterone receptor binding to the 90- and 70-kDa heat shock proteins.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)54835-3 ◽

1991 ◽

Vol 266 (31) ◽

pp. 21165-21173 ◽

Cited By ~ 3

Author(s):

D.B. Schowalter ◽

W.P. Sullivan ◽

N.J. Maihle ◽

A.D. Dobson ◽

O.M. Conneely ◽

...

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Progesterone Receptor ◽

Receptor Binding ◽

Shock Proteins

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Identification and characterization of molecular interactions between mortalin/mtHsp70 and HSP60

Biochemical Journal ◽

10.1042/bj20050861 ◽

2005 ◽

Vol 391 (2) ◽

pp. 185-190 ◽

Cited By ~ 64

Author(s):

Renu Wadhwa ◽

Syuichi Takano ◽

Kamaljit Kaur ◽

Satoshi Aida ◽

Tomoko Yaguchi ◽

...

Keyword(s):

Heat Shock ◽

Molecular Interactions ◽

Heat Shock Protein 60 ◽

Hsp60 Expression ◽

Mitochondrial Hsp70 ◽

Shock Proteins ◽

First Time

Mortalin/mtHsp70 (mitochondrial Hsp70) and HSP60 (heat-shock protein 60) are heat-shock proteins that reside in multiple subcellular compartments, with mitochondria being the predominant one. In the present study, we demonstrate that the two proteins interact both in vivo and in vitro, and that the N-terminal region of mortalin is involved in these interactions. Suppression of HSP60 expression by shRNA (short hairpin RNA) plasmids caused the growth arrest of cancer cells similar to that obtained by suppression of mortalin expression by ribozymes. An overexpression of mortalin, but not of HSP60, extended the in vitro lifespan of normal fibroblasts (TIG-1). Taken together, this study for the first time delineates: (i) molecular interactions of HSP60 with mortalin; (ii) their co- and exclusive localizations in vivo; (iii) their involvement in tumorigenesis; and (iv) their functional distinction in pathways involved in senescence.

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