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Gene Expression and Functional Analysis of Aha1a and Aha1b in Stress Response in Zebrafish

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Abstract

Activator of heat shock protein 90 (hsp90) ATPase (Aha1) is a Hsp90 co-chaperone required for Hsp90 ATPase activation. Aha1 is essential for yeast survival and muscle development in C. elegans under elevated temperature and hsp90-deficeiency induced stress conditions. The roles of Aha1 in vertebrates are poorly understood. Here, we characterized the expression and function of Aha1 in zebrafish. We showed that zebrafish genome contains two aha1 genes, aha1a and aha1b, that show distinct patterns of expression during development. Under the normal physiological conditions, aha1a is primarily expressed in skeletal muscle cells of zebrafish embryos, while aha1b is strongly expressed in the head region. aha1a and aha1b expression increased dramatically in response to heat shock induced stress. In addition, Aha1a-GFP fusion protein exhibited a dynamic translocation in muscle cells in response to heat shock. Moreover, upregulation of aha1 expression was also observed in hsp90a1 knockdown embryos that showed a muscle defect. Genetic studies demonstrated that knockout of aha1a, aha1b or both had no detectable effect on embryonic development, survival, and growth in zebrafish. The aha1a and aha1b mutant embryos showed normal muscle development and stress response in response to heat shock. Single or double aha1a and aha1b mutants could grow into normal reproductive adults with normal skeletal muscle structure and morphology compared with wild type control. Together, data from these studies indicate that Aha1a and Aha1b are involved in stress response. However, they are dispensable in zebrafish embryonic development, growth, and survival.

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References
1.
Wu Y, Zheng X, Ding Y, Zhou M, Wei Z, Liu T . The molecular chaperone Hsp90α deficiency causes retinal degeneration by disrupting Golgi organization and vesicle transportation in photoreceptors. J Mol Cell Biol. 2019; 12(3):216-229. PMC: 7181719. DOI: 10.1093/jmcb/mjz048. View

2.
Du S, Li H, Bian Y, Zhong Y . Heat-shock protein 90alpha1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos. Proc Natl Acad Sci U S A. 2008; 105(2):554-9. PMC: 2206574. DOI: 10.1073/pnas.0707330105. View

3.
Cai M, Si Y, Zhang J, Tian Z, Du S . Zebrafish Embryonic Slow Muscle Is a Rapid System for Genetic Analysis of Sarcomere Organization by CRISPR/Cas9, but Not NgAgo. Mar Biotechnol (NY). 2018; 20(2):168-181. DOI: 10.1007/s10126-018-9794-8. View

4.
Ross C, Poirier M . Protein aggregation and neurodegenerative disease. Nat Med. 2004; 10 Suppl:S10-7. DOI: 10.1038/nm1066. View

5.
Unger A, Beckendorf L, Bohme P, Kley R, von Frieling-Salewsky M, Lochmuller H . Translocation of molecular chaperones to the titin springs is common in skeletal myopathy patients and affects sarcomere function. Acta Neuropathol Commun. 2017; 5(1):72. PMC: 5603016. DOI: 10.1186/s40478-017-0474-0. View