Lux-biosensors for detection of SOS-response, heat shock, and oxidative stress

2010 ◽  
Vol 46 (8) ◽  
pp. 781-788 ◽  
Author(s):  
V. Yu. Kotova ◽  
I. V. Manukhov ◽  
G. B. Zavilgelskii
2019 ◽  
Vol 709 ◽  
pp. 134368 ◽  
Author(s):  
Jonathan Dowell ◽  
Benjamin A. Elser ◽  
Rachel E. Schroeder ◽  
Hanna E. Stevens

1998 ◽  
Vol 9 (6) ◽  
pp. 1339-1349 ◽  
Author(s):  
Kazuhiro Shiozaki ◽  
Mitsue Shiozaki ◽  
Paul Russell

Fission yeast Spc1/StyI MAPK is activated by many environmental insults including high osmolarity, oxidative stress, and heat shock. Spc1/StyI is activated by Wis1, a MAPK kinase (MEK), which is itself activated by Wik1/Wak1/Wis4, a MEK kinase (MEKK). Spc1/StyI is inactivated by the tyrosine phosphatases Pyp1 and Pyp2. Inhibition of Pyp1 was recently reported to play a crucial role in the oxidative stress and heat shock responses. These conclusions were based on three findings: 1) osmotic, oxidative, and heat stresses activate Spc1/StyI in wis4 cells; 2) oxidative stress and heat shock activate Spc1/StyI in cells that express Wis1AA, in which MEKK consensus phosphorylation sites were replaced with alanine; and 3) Spc1/StyI is maximally activated in Δpyp1 cells. Contrary to these findings, we report: 1) Spc1/StyI activation by osmotic stress is greatly reduced in wis4 cells; 2)wis1-AA and Δwis1 cells have identical phenotypes; and 3) all forms of stress activate Spc1/StyI inΔpyp1 cells. We also report that heat shock, but not osmotic or oxidative stress, activate Spc1 in wis1-DDcells, which express Wis1 protein that has the MEKK consensus phosphorylation sites replaced with aspartic acid. Thus osmotic and oxidative stress activate Spc1/StyI by a MEKK-dependent process, whereas heat shock activates Spc1/StyI by a novel mechanism that does not require MEKK activation or Pyp1 inhibition.


1987 ◽  
Vol 33 (2) ◽  
pp. 162-168 ◽  
Author(s):  
M. Kapoor ◽  
J. Lewis

Neurospora crassa cells, grown at 28 °C for 14 h and heat shocked at 48 °C for 45 min, showed the synthesis of 11 heat-shock proteins (nHSPs) in one-dimensional electrophoretic profiles. Treatment with sodium arsenite induced the synthesis of two heat-shock proteins, nHSP70 and nHSP80, and a third, arsenite-specific protein, not induced by hyperthermia. Exposure to 0.5 or 1.0 mM H2O2 led to the induction of two of the heat-inducible nHSP70 family polypeptides. Sodium selenite, used in concert with H2O2, and arsenite were observed to modulate that heat-shock response. In addition, H2O2, menadione, and the glutathione depleters diamide and diethyl maleate promoted the synthesis of another protein, designated oxidative stress-responsive protein (OSP). A DNA-binding protein, specific for Neurospora DNA, was also demonstrated in extracts of heat-shocked cells.


2005 ◽  
Vol 30 (4) ◽  
pp. 499-505 ◽  
Author(s):  
Nand K. Sah ◽  
Shyam Nandan P. Singh ◽  
Sudhir Sahdev ◽  
Sharmishta Banerji ◽  
Vidyanath Jha ◽  
...  

2011 ◽  
Vol 127 (1) ◽  
pp. 228-237 ◽  
Author(s):  
Camila S. Ramos ◽  
Jenicer K.U. Yokoyama-Yasunaka ◽  
Cristina Guerra-Giraldez ◽  
Helen P. Price ◽  
Renato A. Mortara ◽  
...  

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