Oxidative stress triggers aggregation of GFP-tagged Hsp31p, the budding yeast environmental stress response chaperone, and glyoxalase III
Author:
Funder
Polish National Science Center
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Biochemistry
Link
http://link.springer.com/article/10.1007/s12192-017-0868-8/fulltext.html
Reference57 articles.
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2. Antonenkov VD, Grunau S, Ohlmeier S, Hiltunen JK (2010) Peroxisomes are oxidative organelles. Antioxid Redox Signal 13(4):525–537. https://doi.org/10.1089/ars.2009.2996
3. Aslam K, Hazbun TR (2016) Hsp31, a member of the DJ-1 superfamily, is a multitasking stress responder with chaperone activity. Prion 10(2):103–111. https://doi.org/10.1080/19336896.2016.1141858
4. Aslam K, Tsai C-J, Hazbun TR (2016) The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation. Prion 10(6):444–465. https://doi.org/10.1080/19336896.2016.1234574
5. Bankapalli K, Saladi S, Awadia SS et al (2015) Robust glyoxalase activity of Hsp31, a ThiJ/DJ-1/PfpI family member protein, is critical for oxidative stress resistance in Saccharomyces cerevisiae. J Biol Chem 290(44):26491–26507. https://doi.org/10.1074/jbc.M115.673624
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