Stage-specific localization of the small heat shock protein Hsp27 during oogenesis in Drosophila melanogaster

Chromosoma ◽  
1996 ◽  
Vol 105 (3) ◽  
pp. 142-149 ◽  
Author(s):  
R. Marin ◽  
R. M. Tanguay
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Specific Localization

scholarly journals Perturbation of chromatin architecture on ecdysterone induction of Drosophila melanogaster small heat shock protein genes.

1989 ◽  
Vol 9 (1) ◽  
pp. 332-335 ◽  
Author(s):  
S E Kelly ◽  
I L Cartwright
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Intergenic Region ◽  
Small Heat Shock Protein ◽  
Dnase I ◽  
Developmentally Regulated ◽  
Regulatory Interactions ◽  
Chromatin Architecture ◽  
Heat Shock Protein Genes

Alterations in the pattern of DNase I hypersensitivity were observed on ecdysterone-stimulated transcription of Drosophila melanogaster small heat shock protein genes. Perturbations were induced near hsp27 and hsp22, coupled with an extensive domain of chromatin unfolding in the intergenic region between hsp23 and the developmentally regulated gene 1. These regions represent candidates for ecdysterone regulatory interactions.

scholarly journals Small heat shock protein Hsp67Bc plays a significant role in Drosophila melanogaster cold stress tolerance

2020 ◽  
Vol 223 (21) ◽  
pp. jeb219592
Author(s):  
Dina Malkeyeva ◽  
Elena Kiseleva ◽  
Svetlana Fedorova
Keyword(s):  
Drosophila Melanogaster ◽  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cold Stress ◽  
Stress Tolerance ◽  
Developmental Stages ◽  
Small Heat Shock Protein ◽  
Recovery Phase ◽  
Main Function

ABSTRACTHsp67Bc in Drosophila melanogaster is a member of the small heat shock protein family, the main function of which is to prevent the aggregation of misfolded or damaged proteins. Hsp67Bc interacts with Starvin and Hsp23, which are known to be a part of the cold stress response in the fly during the recovery phase. In this study, we investigated the role of the Hsp67Bc gene in the cold stress response. We showed that in adult Drosophila, Hsp67Bc expression increases after cold stress and decreases after 1.5 h of recovery, indicating the involvement of Hsp67Bc in short-term stress recovery. We also implemented a deletion in the D. melanogaster Hsp67Bc gene using imprecise excision of a P-element, and analysed the cold tolerance of Hsp67Bc-null mutants at different developmental stages. We found that Hsp67Bc-null homozygous flies are viable and fertile but display varying cold stress tolerance throughout the stages of ontogenesis: the survival after cold stress is slightly impaired in late third instar larvae, unaffected in pupae, and notably affected in adult females. Moreover, the recovery from chill coma is delayed in Hsp67Bc-null adults of both sexes. In addition, the deletion in the Hsp67Bc gene caused more prominent up-regulation of Hsp70 following cold stress, suggesting the involvement of Hsp70 in compensation of the lack of the Hsp67Bc protein. Taken together, our results suggest that Hsp67Bc is involved in the recovery of flies from a comatose state and contributes to the protection of the fruit fly from cold stress.

Perturbation of chromatin architecture on ecdysterone induction of Drosophila melanogaster small heat shock protein genes

1989 ◽  
Vol 9 (1) ◽  
pp. 332-335
Author(s):  
S E Kelly ◽  
I L Cartwright
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Intergenic Region ◽  
Small Heat Shock Protein ◽  
Dnase I ◽  
Developmentally Regulated ◽  
Regulatory Interactions ◽  
Chromatin Architecture ◽  
Heat Shock Protein Genes

Alterations in the pattern of DNase I hypersensitivity were observed on ecdysterone-stimulated transcription of Drosophila melanogaster small heat shock protein genes. Perturbations were induced near hsp27 and hsp22, coupled with an extensive domain of chromatin unfolding in the intergenic region between hsp23 and the developmentally regulated gene 1. These regions represent candidates for ecdysterone regulatory interactions.

scholarly journals Identification of proteins interacting with the mitochondrial small heat shock protein Hsp22 of Drosophila melanogaster: Implication in mitochondrial homeostasis

PLoS ONE ◽  
2018 ◽  
Vol 13 (3) ◽  
pp. e0193771 ◽  
Author(s):  
Afrooz Dabbaghizadeh ◽  
Geneviève Morrow ◽  
Yasmine Ould Amer ◽  
Etienne Hebert Chatelain ◽  
Nicolas Pichaud ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Mitochondrial Homeostasis

scholarly journals Oligomerization and chaperone-like activity of Drosophila melanogaster small heat shock protein DmHsp27 and three arginine mutants in the alpha-crystallin domain

2016 ◽  
Vol 22 (4) ◽  
pp. 455-466 ◽  
Author(s):  
Mohamed Taha Moutaoufik ◽  
Geneviève Morrow ◽  
Halim Maaroufi ◽  
Céline Férard ◽  
Stéphanie Finet ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Alpha Crystallin

scholarly journals Effect of N-terminal region of nuclear Drosophila melanogaster small heat shock protein DmHsp27 on function and quaternary structure

PLoS ONE ◽  
2017 ◽  
Vol 12 (5) ◽  
pp. e0177821 ◽  
Author(s):  
Mohamed Taha Moutaoufik ◽  
Geneviève Morrow ◽  
Stéphanie Finet ◽  
Robert M. Tanguay
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Quaternary Structure ◽  
Small Heat Shock Protein ◽  
Terminal Region

scholarly journals Maternal loading of a small heat shock protein increases embryo thermal tolerance in Drosophila melanogaster

2017 ◽  
Author(s):  
Brent L. Lockwood ◽  
Cole R. Julick ◽  
Kristi L. Montooth
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Maternal Effects ◽  
Thermal Tolerance ◽  
Maternal Investment ◽  
Small Heat Shock Protein ◽  
Larval Performance ◽  
Offspring Survival

ABSTRACTMaternal investment is likely to have direct effects on offspring survival. In oviparous animals whose embryos are exposed to the external environment, maternal provisioning of molecular factors like mRNAs and proteins may help embryos cope with sudden changes in the environment. Here we sought to modify the maternal mRNA contribution to offspring embryos and test for maternal effects on acute thermal tolerance in early embryos of Drosophila melanogaster. We drove in vivo overexpression of a small heat shock protein gene (Hsp23) in female ovaries and measured the effects of acute thermal stress on offspring embryonic survival and larval development. We report that overexpression of the Hsp23 gene in female ovaries produced offspring embryos with increased thermal tolerance. We also found that brief heat stress in the early embryonic stage (0 to 1 hour-old) caused decreased larval performance later in life (5 to 10 days-old), as indexed by pupation height, as well as increased development time to pupation. Maternal overexpression of Hsp23 protected embryos against these heat-induced larval defects. Our data demonstrate that transient products of single genes have large and lasting effects on whole-organism environmental tolerance. Further, our results suggest that maternal effects have a profound impact on offspring survival in the context of thermal variability.SUMMARY STATEMENTA gene-specific maternal effect confers thermal tolerance to offspring embryos in the fruit fly Drosophila melanogaster.

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