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The NADP+-dependent glutamate dehydrogenase Gdh1 is subjected to glucose starvation-induced reversible aggregation that affects stress resistance in yeast
Woo Hyun Lee , Ju Yeong Oh , Pil Jae Maeng
J. Microbiol. 2019;57(10):884-892.   Published online August 3, 2019
DOI: https://doi.org/10.1007/s12275-019-9065-z
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AbstractAbstract
The yeast Saccharomyces cerevisiae has two isoforms of NADP+-dependent glutamate dehydrogenase (Gdh1 and Gdh3) that catalyze the synthesis of glutamate from α-ketoglutarate and NH4 +. In the present study, we confirmed that Gdh3, but not Gdh1, mainly contributes to the oxidative stress resistance of stationary-phase cells and found evidence suggesting that the insignificance of Gdh1 to stress resistance is possibly resulted from conditional and reversible aggregation of Gdh1 into punctuate foci initiated in parallel with postdiauxic growth. Altered localization to the mitochondria or peroxisomes prevented Gdh1, which was originally localized in the cytoplasm, from stationary phase-specific aggregation, suggesting that some cytosolic factors are involved in the process of Gdh1 aggregation. Glucose starvation triggered the transition of the soluble form of Gdh1 into the insoluble aggregate form, which could be redissolved by replenishing glucose, without any requirement for protein synthesis. Mutational analysis showed that the N-terminal proximal region of Gdh1 (NTP1, aa 21-26, TLFEQH) is essential for glucose starvation-induced aggregation. We also found that the substitution of NTP1 with the corresponding region of Gdh3 (NTP3) significantly increased the contribution of the mutant Gdh1 to the stress resistance of stationary-phase cells. Thus, this suggests that NTP1 is responsible for the negligible role of Gdh1 in maintaining the oxidative stress resistance of stationary- phase cells and the stationary phase-specific stresssensitive phenotype of the mutants lacking Gdh3.

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  • Genomic characterization of denitrifying methylotrophic Pseudomonas aeruginosa strain AAK/M5 isolated from municipal solid waste landfill soil
    Ashish Kumar Singh, Rakesh Kumar Gupta, Hemant J. Purohit, Anshuman Arun Khardenavis
    World Journal of Microbiology and Biotechnology.2022;[Epub]     CrossRef
  • Effects of Molecular Crowding and Betaine on HSPB5 Interactions, with Target Proteins Differing in the Quaternary Structure and Aggregation Mechanism
    Vera A. Borzova, Svetlana G. Roman, Anastasiya V. Pivovarova, Natalia A. Chebotareva
    International Journal of Molecular Sciences.2022; 23(23): 15392.     CrossRef
Research Support, Non-U.S. Gov't
Growth Phase-dependent Roles of Sir2 in Oxidative Stress Resistance and Chronological Lifespan in Yeast
Woo Kyu Kang , Yeong Hyeock Kim , Byoung-Soo Kim , Jeong-Yoon Kim
J. Microbiol. 2014;52(8):652-658.   Published online July 5, 2014
DOI: https://doi.org/10.1007/s12275-014-4173-2
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  • 9 Crossref
AbstractAbstract
Silent Information Regulator 2 (Sir2), a conserved NAD+- dependent histone deacetylase, has been implicated as one of the key factors in regulating stress response and longevity. Here, we report that the role of Sir2 in oxidative stress resistance and chronological lifespan is dependent on growth phase in yeast. In exponential phase, sir2Δ cells were more resistant to H2O2 stress and had a longer chronological lifespan than wild type. By contrast, in post-diauxic phase, sir2Δ cells were less resistant to H2O2 stress and had a shorter chronological lifespan than wild type cells. Similarly, the expression of antioxidant genes, which are essential to cope with oxidative stress, was regulated by Sir2 in a growth phasedependent manner. Collectively, our findings highlight the importance of the metabolic state of the cell in determining whether Sir2 can protect against or accelerate cellular aging of yeast.

Citations

Citations to this article as recorded by  
  • RNA-sequencing exploration on SIR2 and SOD genes in Polyalthia longifolia leaf methanolic extracts (PLME) mediated anti-aging effects in Saccharomyces cerevisiae BY611 yeast cells
    Manisekaran Hemagirri, Yeng Chen, Subash C. B. Gopinath, Mohd Adnan, Mitesh Patel, Sreenivasan Sasidharan
    Biogerontology.2024; 25(4): 705.     CrossRef
  • The intricate role of Sir2 in oxidative stress response during the post-diauxic phase in Saccharomyces cerevisiae
    Yeong Hyeock Kim, Ji-In Ryu, Mayur Nimbadas Devare, Juhye Jung, Jeong-Yoon Kim
    Frontiers in Microbiology.2023;[Epub]     CrossRef
  • Inactivation of MrSir2 in Monascus ruber Influenced the Developmental Process and the Production of Monascus Azaphilone Pigments
    Jing Zhang, Yudan Yang, Zejing Mao, Qingqing Yan, Qi Chen, Ming Yi, Yanchun Shao
    Applied Biochemistry and Biotechnology.2022; 194(12): 5702.     CrossRef
  • Histone deacetylase SirE regulates development, DNA damage response and aflatoxin production in Aspergillus flavus
    Meifang Wen, Huahui Lan, Ruilin Sun, Xuan Chen, Xin Zhang, Zhuo Zhu, Can Tan, Jun Yuan, Shihua Wang
    Environmental Microbiology.2022; 24(11): 5596.     CrossRef
  • Differential protein expression and post-translational modifications in metronidazole-resistant Giardia duodenalis
    Samantha J Emery, Louise Baker, Brendan R E Ansell, Mehdi Mirzaei, Paul A Haynes, Malcom J McConville, Staffan G Svärd, Aaron R Jex
    GigaScience.2018;[Epub]     CrossRef
  • HST1 increases replicative lifespan of a sir2Δ mutant in the absence of PDE2 in Saccharomyces cerevisiae
    Woo Kyu Kang, Mayur Devare, Jeong-Yoon Kim
    Journal of Microbiology.2017; 55(2): 123.     CrossRef
  • Sirt1: Role Under the Condition of Ischemia/Hypoxia
    Xiaofei Meng, Jin Tan, Mengmeng Li, Shuling Song, Yuyang Miao, Qiang Zhang
    Cellular and Molecular Neurobiology.2017; 37(1): 17.     CrossRef
  • A haploproficient interaction of the transaldolase paralogue NQM1 with the transcription factor VHR1 affects stationary phase survival and oxidative stress resistance
    Steve Michel, Markus A Keller, Mirjam MC Wamelink, Markus Ralser
    BMC Genetics.2015;[Epub]     CrossRef
  • Sir2 phosphorylation through cAMP-PKA and CK2 signaling inhibits the lifespan extension activity of Sir2 in yeast
    Woo Kyu Kang, Yeong Hyeock Kim, Hyun Ah Kang, Ki-Sun Kwon, Jeong-Yoon Kim
    eLife.2015;[Epub]     CrossRef

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