MTM1 plays an important role in the regulation of zinc tolerance in Saccharomyces cerevisiae.

作者: Lingyun Wang , Xiaobin Wu , Nathan Simth , Lingzhi Zhang , Jiang Bian

DOI: 10.1016/J.JTEMB.2021.126759

关键词:

摘要: Abstract Background Acquisition and distribution of zinc supports a number biological processes. Various molecular factors are involved in metabolism but not fully explored. Basic procedures Spontaneous mutants were generated yeast with excess culture followed by whole genome DNA sequencing to discover related genes bioinformatics. An identified mutant was characterized through metallomic biology methods. Main findings Here we reported that MTM1 knockout cells displayed much stronger tolerance than wild type on SC medium when exposed zinc. Zn accumulation mtm1Δ dramatically decreased compared under excessive condition due deletion reduced uptake. ZRC1 mRNA level significantly higher the wild-type strain leading increased vacuolar accumulations cells. The levels ZRT1 ZAP1 contributing less zrc1Δmtm1Δ double exhibited sensitivity. did afford resistance an effect mediated influence ROS. Superoxide dismutase 2 (Sod2p) activity severely impaired restored supplementation. Meanwhile, additional showed no significant localization expression Mtm1p. Principal conclusions Our study reveals gene plays important role regulation homeostasis via changing uptake distribution. This discovery provides new insights for better understanding biochemical communication between vacuole mitochondrial relation zinc-metabolism.

参考文章(43)
Mark S. Longtine, Amos Mckenzie III, Douglas J. Demarini, Nirav G. Shah, Achim Wach, Arndt Brachat, Peter Philippsen, John R. Pringle, Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae Yeast. ,vol. 14, pp. 953- 961 ,(1998) , 10.1002/(SICI)1097-0061(199807)14:10<953::AID-YEA293>3.0.CO;2-U
H. Zhao, D. Eide, The yeast ZRT1 gene encodes the zinc transporter protein of a high-affinity uptake system induced by zinc limitation. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 93, pp. 2454- 2458 ,(1996) , 10.1073/PNAS.93.6.2454
Florian L. Muller, Yuhong Liu, Holly Van Remmen, Complex III Releases Superoxide to Both Sides of the Inner Mitochondrial Membrane Journal of Biological Chemistry. ,vol. 279, pp. 49064- 49073 ,(2004) , 10.1074/JBC.M407715200
Elena Wiederhold, Tejas Gandhi, Hjalmar P. Permentier, Rainer Breitling, Bert Poolman, Dirk J. Slotboom, The Yeast Vacuolar Membrane Proteome Molecular & Cellular Proteomics. ,vol. 8, pp. 380- 392 ,(2009) , 10.1074/MCP.M800372-MCP200
Zhao Su, Mao-Feng Chai, Ping-Li Lu, Rui An, Jia Chen, Xue-Chen Wang, AtMTM1, a novel mitochondrial protein, may be involved in activation of the manganese-containing superoxide dismutase in Arabidopsis. Planta. ,vol. 226, pp. 1031- 1039 ,(2007) , 10.1007/S00425-007-0547-6
R. J. Cousins, R. K. Blanchard, M. P. Popp, L. Liu, J. Cao, J. B. Moore, C. L. Green, A global view of the selectivity of zinc deprivation and excess on genes expressed in human THP-1 mononuclear cells Proceedings of the National Academy of Sciences of the United States of America. ,vol. 100, pp. 6952- 6957 ,(2003) , 10.1073/PNAS.0732111100
Amornrat Naranuntarat, Laran T. Jensen, Samuel Pazicni, James E. Penner-Hahn, Valeria C. Culotta, The interaction of mitochondrial iron with manganese superoxide dismutase. Journal of Biological Chemistry. ,vol. 284, pp. 22633- 22640 ,(2009) , 10.1074/JBC.M109.026773
Mei M. Whittaker, Aravind Penmatsa, James W. Whittaker, The Mtm1p carrier and pyridoxal 5'-phosphate cofactor trafficking in yeast mitochondria. Archives of Biochemistry and Biophysics. ,vol. 568, pp. 64- 70 ,(2015) , 10.1016/J.ABB.2015.01.021
Hiroyuki Yanagisawa, Takashi Miyazaki, Makoto Nodera, Yuka Miyajima, Takashi Suzuki, Takamasa Kido, Machi Suka, Zinc-Excess Intake Causes the Deterioration of Renal Function Accompanied by an Elevation in Systemic Blood Pressure Primarily Through Superoxide Radical-Induced Oxidative Stress. International Journal of Toxicology. ,vol. 33, pp. 288- 296 ,(2014) , 10.1177/1091581814532958