Sequence requirements for upregulated expression of Drosophila hsp70 transgenes during aging - PubMed (original) (raw)
Sequence requirements for upregulated expression of Drosophila hsp70 transgenes during aging
J C Wheeler et al. Neurobiol Aging. 1999 Sep-Oct.
Abstract
hsp70 protein and hsp70:lacZ fusion reporters are upregulated during aging and in response to oxidative stress in the thorax of Drosophila. hsp70 expression was increased during aging in each of seven different Drosophila genetic backgrounds tested, 2.6-4.8-fold. DNA sequence requirements were investigated by analysis of nine distinct hsp70:lacZ fusion reporter constructs in multiple independent transgenic lines. hsp70 sequences -194 to +276 supported an average 2.7-fold increase during aging. This increase was reduced or eliminated by deletion or point mutation of the heat shock response elements, consistent with a transcriptional mechanism. Similar sequence requirements were observed for increased expression in response to catalase null mutation as a model of oxidative stress. hsp70 5'UTR sequences were required for efficient basal expression of transgenes, but were not sufficient to confer detectable upregulation during aging. Inclusion of additional hsp70 coding region sequences from +276 to + 1011 created a larger hsp70:lacZ fusion protein and had two effects: dramatic reduction of the overall expression level of the fusion protein, and an additional three to fourfold upregulation during aging. These results suggest that the coding region sequences reduce fusion protein abundance and that this negative effect decreases as a function of age. The data support a model for increased expression of hsp70 transgenes during aging involving both transcriptional and posttranscriptional components.
Similar articles
- Muscle-specific expression of Drosophila hsp70 in response to aging and oxidative stress.
Wheeler JC, Bieschke ET, Tower J. Wheeler JC, et al. Proc Natl Acad Sci U S A. 1995 Oct 24;92(22):10408-12. doi: 10.1073/pnas.92.22.10408. Proc Natl Acad Sci U S A. 1995. PMID: 7479794 Free PMC article. - Regulation of heat shock proteins, Hsp70 and Hsp64, in heat-shocked Malpighian tubules of Drosophila melanogaster larvae.
Lakhotia SC, Srivastava P, Prasanth KV. Lakhotia SC, et al. Cell Stress Chaperones. 2002 Oct;7(4):347-56. doi: 10.1379/1466-1268(2002)007<0347:rohsph>2.0.co;2. Cell Stress Chaperones. 2002. PMID: 12653479 Free PMC article. - Detection and analysis of somatic mutations at a lacZ reporter locus in higher organisms: application to Mus musculus and Drosophila melanogaster.
Garcia AM, Busuttil RA, Rodriguez A, Cabrera C, Lundell M, Dollé ME, Vijg J. Garcia AM, et al. Methods Mol Biol. 2007;371:267-87. doi: 10.1007/978-1-59745-361-5_20. Methods Mol Biol. 2007. PMID: 17634588 Review. - Mutation accumulation in vivo and the importance of genome stability in aging and cancer.
Dollé ME, Giese H, van Steeg H, Vijg J. Dollé ME, et al. Results Probl Cell Differ. 2000;29:165-80. doi: 10.1007/978-3-540-48003-7_9. Results Probl Cell Differ. 2000. PMID: 10838700 Review. No abstract available.
Cited by
- Markers and mechanisms of death in Drosophila.
Tower J. Tower J. Front Aging. 2023 Dec 12;4:1292040. doi: 10.3389/fragi.2023.1292040. eCollection 2023. Front Aging. 2023. PMID: 38149028 Free PMC article. - Transcription dynamics of heat-shock proteins (Hsps) and endosymbiont titres in response to thermal stress in whitefly, Bemisia tabaci (Asia-I).
Barman M, Samanta S, Ahmed B, Dey S, Chakraborty S, Deeksha MG, Dutta S, Samanta A, Tarafdar J, Roy D. Barman M, et al. Front Physiol. 2023 Jan 13;13:1097459. doi: 10.3389/fphys.2022.1097459. eCollection 2022. Front Physiol. 2023. PMID: 36714306 Free PMC article. - Expression of Heat Shock Protein 70 Is Insufficient To Extend Drosophila melanogaster Longevity.
Xiao C, Hull D, Qiu S, Yeung J, Zheng J, Barwell T, Robertson RM, Seroude L. Xiao C, et al. G3 (Bethesda). 2019 Dec 3;9(12):4197-4207. doi: 10.1534/g3.119.400782. G3 (Bethesda). 2019. PMID: 31624139 Free PMC article. - dFOXO Activates Large and Small Heat Shock Protein Genes in Response to Oxidative Stress to Maintain Proteostasis in Drosophila.
Donovan MR, Marr MT 2nd. Donovan MR, et al. J Biol Chem. 2016 Sep 2;291(36):19042-50. doi: 10.1074/jbc.M116.723049. Epub 2016 Jul 19. J Biol Chem. 2016. PMID: 27435672 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Medical
Molecular Biology Databases