Phenological Asynchrony Is Associated With Diapause Program and Heat Shock Protein Expression in Three Grasshopper Species in the Inner Mongolian Steppe

Phenological asynchrony is a common and important natural phenomenon that affects interspecific interaction, resource allocation, species survival, and range shift in sympatric species. However, the underpinnings for regulating phenological asynchrony at physiological and molecular levels remains less explored. We investigated the seasonal pattern of emergence period and abundance in three dominant grasshopper species, namely, Dasyhipus barbipes, Oedalus asiaticus, and Chorthippus dubius, which occur sympatrically in the Inner Mongolian steppe. The three grasshopper species decoupled their population occurrence phenology that occurred in a growing season between May and September and diverged into early, middle, and late seasonal species. We also examined the association of embryonic diapause and heat shock protein (Hsp) expression with phenological asynchrony in the three species. The species developed different embryonic diapause programs, i.e., obligate diapause, facultative diapause, and non-diapause, to control the timing of egg hatching and seasonality of population occurrence. The diapausing eggs exhibited significantly enhanced supercooling capacity compared with pre- and post-diapausing eggs. Gene expression analysis in the developmental process revealed that three Hsps, e.g., Hsp20.6, Hsp40, and Hsp90, were significantly upregulated in diapause state relative to that in pre- and post-diapause states; expression of these genes seems to be associated with the diapause program regulation. This study provides a possible mechanistic explanation for phenological differentiation among sympatric species in a typical steppe habitat and establishes a potential linkage among phenological asynchrony, diapause, and Hsp gene expression. The findings will facilitate our prediction of population dynamics and pest management.

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Study of Heat Shock Protein (Hsp) 70 gene expression of Emilia sonchifolia L. and Sphagneticola trilobata L. in Universitas Indonesia, Depok and Kebun Raya Cibodas

Journal of Physics Conference Series ◽

10.1088/1742-6596/1725/1/012047 ◽

2021 ◽

Vol 1725 ◽

pp. 012047

Author(s):

M Syadewi ◽

A Salamah ◽

A E Maryanto ◽

N Andayani

Keyword(s):

Gene Expression ◽

Heat Shock ◽

Heat Shock Protein ◽

Hsp 70

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Heat Shock Protein 70 Improves In Vitro Embryo Yield and Quality from Heat Stressed Bovine Oocytes

Animals ◽

10.3390/ani11061794 ◽

2021 ◽

Vol 11 (6) ◽

pp. 1794

Author(s):

Konstantina Stamperna ◽

Themistoklis Giannoulis ◽

Eleni Dovolou ◽

Maria Kalemkeridou ◽

Ioannis Nanas ◽

...

Keyword(s):

Gene Expression ◽

Heat Shock ◽

Heat Shock Protein ◽

Heat Shock Protein 70 ◽

Cumulus Cells ◽

Intramolecular Interactions ◽

Developmental Competence ◽

Embryo Yield ◽

Bovine Oocytes

Heat shock protein 70 (HSP70) is a chaperon that stabilizes unfolded or partially folded proteins, preventing inappropriate inter- and intramolecular interactions. Here, we examined the developmental competence of in vitro matured oocytes exposed to heat stress with or without HSP70. Bovine oocytes were matured for 24 h at 39 °C without (group C39) or with HSP70 (group H39) and at 41 °C for the first 6 h, followed by 16 h at 39 °C with (group H41) or without HSP70 (group C41). After insemination, zygotes were cultured for 9 days at 39 °C. Cleavage and embryo yield were assessed 48 h post insemination and on days 7, 8, 9, respectively. Gene expression was assessed by RT-PCR in oocytes, cumulus cells and blastocysts. In C41, blastocysts formation rate was lower than in C39 and on day 9 it was lower than in H41. In oocytes, HSP70 enhanced the expression of three HSP genes regardless of incubation temperature. HSP70 at 39 °C led to tight coordination of gene expression in oocytes and blastocysts, but not in cumulus cells. Our results imply that HSP70, by preventing apoptosis, supporting signal transduction, and increasing antioxidant protection of the embryo, protects heat stressed maturing bovine oocyte and restores its developmental competence.

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Ribosome Profiling Reveals HSP90 Inhibitor Effects on Stage-Specific Protein Synthesis in Leishmania donovani

mSystems ◽

10.1128/msystems.00214-18 ◽

2018 ◽

Vol 3 (6) ◽

Cited By ~ 10

Author(s):

Eugenia Bifeld ◽

Stephan Lorenzen ◽

Katharina Bartsch ◽

Juan-José Vasquez ◽

T. Nicolai Siegel ◽

...

Keyword(s):

Gene Expression ◽

Protein Synthesis ◽

Heat Shock ◽

Heat Shock Protein ◽

Leishmania Donovani ◽

Specific Protein ◽

Ribosome Profiling ◽

Severe Illness ◽

Content Type ◽

Hsp90 Activity

ABSTRACT The 90-kDa heat shock protein (HSP90) of eukaryotes is a highly abundant and essential chaperone required for the maturation of regulatory and signal proteins. In the protozoan parasite Leishmania donovani, causative agent of the fatal visceral leishmaniasis, HSP90 activity is essential for cell proliferation and survival. Even more importantly, its inhibition causes life cycle progression from the insect stage to the pathogenic, mammalian stage. To unravel the molecular impact of HSP90 activity on the parasites’ gene expression, we performed a ribosome profiling analysis of L. donovani, comparing genome-wide protein synthesis patterns in the presence and absence of the HSP90-specific inhibitor radicicol and an ectopically expressed radicicol-resistant HSP90 variant. We find that ribosome-protected RNA faithfully maps open reading frames and represents 97% of the annotated protein-coding genes of L. donovani. Protein synthesis was found to correlate poorly with RNA steady-state levels, indicating a regulated translation as primary mechanism for HSP90-dependent gene expression. The results confirm inhibitory effects of HSP90 on the synthesis of Leishmania proteins that are associated with the pathogenic, intracellular stage of the parasite. Those include heat shock proteins, redox enzymes, virulence-enhancing surface proteins, proteolytic pathways, and a complete set of histones. Conversely, HSP90 promotes fatty acid synthesis enzymes. Complementing radicicol treatment with the radicicol-resistant HSP90rr variant revealed important off-target radicicol effects that control a large number of the above-listed proteins. Leishmania lacks gene-specific transcription regulation and relies on regulated translation instead. Our ribosome footprinting analysis demonstrates a controlling function of HSP90 in stage-specific protein synthesis but also significant, HSP90-independent effects of the inhibitor radicicol. IMPORTANCE Leishmania parasites cause severe illness in humans and animals. They exist in two developmental stages, insect form and mammalian form, which differ in shape and gene expression. By mapping and quantifying RNA fragments protected by protein synthesis complexes, we determined the rates of protein synthesis for >90% of all Leishmania proteins in response to the inhibition of a key regulatory protein, the 90-kDa heat shock protein. We find that Leishmania depends on a regulation of protein synthesis for controlling its gene expression and that heat shock protein 90 inhibition can trigger the developmental program from insect form to mammalian form of the pathogen.

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