Stress-driven dynamic regulation of multiple tolerance genes improves robustness and productive capacity of Saccharomyces cerevisiae in industrial lignocellulose fermentation

2020 ◽  
Vol 61 ◽  
pp. 160-170 ◽  
Author(s):  
Lei Qin ◽  
Shuxin Dong ◽  
Jie Yu ◽  
Xiaoyu Ning ◽  
Ke Xu ◽  
...  
2017 ◽  
Vol 16 (1) ◽  
Author(s):  
Paulo Gonçalves Teixeira ◽  
Raphael Ferreira ◽  
Yongjin J. Zhou ◽  
Verena Siewers ◽  
Jens Nielsen

Genetics ◽  
2008 ◽  
Vol 178 (2) ◽  
pp. 693-701 ◽  
Author(s):  
Stephanie Smith ◽  
Soma Banerjee ◽  
Regina Rilo ◽  
Kyungjae Myung

1995 ◽  
Vol 15 (10) ◽  
pp. 5470-5481 ◽  
Author(s):  
A Ferrando ◽  
S J Kron ◽  
G Rios ◽  
G R Fink ◽  
R Serrano

Dynamic regulation of ion transport is essential for homeostasis as cells confront changes in their environment. The gene HAL3 encodes a novel component of this regulatory circuit in the yeast Saccharomyces cerevisiae. Overexpression of HAL3 improves growth of wild-type cells exposed to toxic concentrations of sodium and lithium and suppresses the salt sensitivity conferred by mutation of the calcium-dependent protein phosphatase calcineurin. Null mutants of HAL3 display salt sensitivity. The sequence of HAL3 gives little clue to its function. However, alterations in intracellular cation concentrations associated with changes in HAL3 expression suggest that HAL3 activity may directly increase cytoplasmic K+ and decrease Na+ and Li+. Cation efflux in S. cerevisiae is mediated by the P-type ATPase encoded by the ENA1/PMR24 gene, a putative plasma membrane Na+ pump whose expression is salt induced. Acting in concert with calcineurin, HAL3 is necessary for full activation of ENA1 expression. This functional complementarity is also reflected in the participation of both proteins in recovery from alpha-factor-induced growth arrest. Recently, HAL3 was isolated as a gene (named SIS2) which when overexpressed partially relieves loss of transcription of G1 cyclins in mutants lacking the protein phosphatase Sit4p. Therefore, HAL3 influences cell cycle control and ion homeostasis, acting in parallel to the protein phosphatases Sit4p and calcineurin.


Microbiology ◽  
2011 ◽  
Vol 157 (12) ◽  
pp. 3500-3511 ◽  
Author(s):  
Jarne Postmus ◽  
Işil Tuzun ◽  
Martijn Bekker ◽  
Wally H. Müller ◽  
M. Joost Teixeira de Mattos ◽  
...  

To adapt to changes in the environment, cells have to dynamically alter their phenotype in response to, for instance, temperature and oxygen availability. Interestingly, mitochondrial function in Saccharomyces cerevisiae is inherently temperature sensitive; above 37 °C, yeast cells cannot grow on respiratory carbon sources. To investigate this phenomenon, we studied the effect of cultivation temperature on the efficiency (production of ATP per atom of oxygen consumed, or P/O) of the yeast respiratory chain in glucose-limited chemostats. We determined that even though the specific oxygen consumption rate did not change with temperature, oxygen consumption no longer contributed to mitochondrial ATP generation at temperatures higher than 37 °C. Remarkably, between 30 and 37 °C, we observed a linear increase in respiratory efficiency with growth temperature, up to a P/O of 1.4, close to the theoretical maximum that can be reached in vivo. The temperature-dependent increase in efficiency required the presence of the mitochondrial glycerol-3-phosphate dehydrogenase GUT2. Respiratory chain efficiency was also altered in response to changes in oxygen availibility. Our data show that, even in the absence of alternative oxidases or uncoupling proteins, yeast has retained the ability to dynamically regulate the efficiency of coupling of oxygen consumption to proton translocation in the respiratory chain in response to changes in the environment.


2001 ◽  
Vol 36 (2) ◽  
pp. 196-201 ◽  
Author(s):  
F. Seibold ◽  
O. Stich ◽  
R. Hufnagl ◽  
S. Kamil ◽  
M. Scheurlen

2007 ◽  
Vol 45 (08) ◽  
Author(s):  
S Schmechel ◽  
V Schachinger ◽  
F Seibold ◽  
C Tillack ◽  
T Ochsenkühn ◽  
...  

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