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Proteomic Evaluation of Cellular Responses of Saccharomyces cerevisiae to Formic Acid Stress

  • Lee, Sung-Eun (Research Station, Nanotoxtech Inc.) ;
  • Park, Byeoung-Soo (Research Station, Nanotoxtech Inc.) ;
  • Yoon, Jeong-Jun (Eco Technology Center, Chungcheong Gangwon Technology Application Division, Korea Institute of Industrial Technology (KITECH))
  • Received : 2010.11.15
  • Accepted : 2010.11.25
  • Published : 2010.12.31

Abstract

Formic acid is a representative carboxylic acid that inhibits bacterial cell growth, and thus it is generally considered to constitute an obstacle to the reuse of renewable biomass. In this study, Saccharomyces cerevisiae was used to elucidate changes in protein levels in response to formic acid. Fifty-seven differentially expressed proteins in response to formic acid toxicity in S. cerevisiae were identified by 1D-PAGE and nano-liquid chromatography-tandem mass spectrometry (nano-LC-MS/MS) analyses. Among the 28 proteins increased in expression, four were involved in the MAP kinase signal transduction pathway and one in the oxidative stress-induced pathway. A dramatic increase was observed in the number of ion transporters related to maintenance of acid-base balance. Regarding the 29 proteins decreased in expression, they were found to participate in transcription during cell division. Heat shock protein 70, glutathione reductase, and cytochrome c oxidase were measured by LC-MS/MS analysis. Taken together, the inhibitory action of formic acid on S. cerevisiae cells might disrupt the acidbase balance across the cell membrane and generate oxidative stress, leading to repressed cell division and death. S. cerevisiae also induced expression of ion transporters, which may be required to maintain the acid-base balance when yeast cells are exposed to high concentrations of formic acid in growth medium.

Keywords

References

  1. Cardona CA, Quintero JA, Paz IC. Production of bioethanol from sugarcane bagasse: status and perspectives. Bioresour Technol 2010;101:4754-66. https://doi.org/10.1016/j.biortech.2009.10.097
  2. Binod P, Sindhu R, Singhania RR, Vikram S, Devi L, Nagalakshmi S, Kurien N, Sukumaran RK, Pandey A. Bioethanol production from rice straw: an overview. Bioresour Technol 2010;101:4767-74. https://doi.org/10.1016/j.biortech.2009.10.079
  3. Jojensen H, Sanadi AR, Felby C, Lange NE, Fischer M, Ernst S. Production of ethanol and feed by high dry matter hydrolysis and fermentation of palm kernel press cake. Appl Biochem Biotechnol 2010;161:318-32. https://doi.org/10.1007/s12010-009-8814-6
  4. Li X, Kim TH, Nghiem NP. Bioethanol production from corn stover using aqueous ammonia pretreatment and two-phase simultaneous saccharification and fermentation (TPSSF). Bioresour Technol 2010;101:5910-6. https://doi.org/10.1016/j.biortech.2010.03.015
  5. Sorensen A, Teller PJ, Hilstrom T, Ahring BK. Hydrolysis of Miscanthus for bioethanol production using dilute acid presoaking combined with wet explosion pre-treatment and enzymatic treatment. Bioresour Technol 2008;99:6602-7. https://doi.org/10.1016/j.biortech.2007.09.091
  6. Keshwani DR, Cheng JJ. Switchgrass for bioethanol and other value-added applications: a review. Bioresour Technol 2009;100:1515-23. https://doi.org/10.1016/j.biortech.2008.09.035
  7. Sudesh K, Abe H, Doi Y. Synthesis, structure and properties of polyhydroxyalkanoates: biological polyesters. Prog Polym Sci 2000;25:1503-55. https://doi.org/10.1016/S0079-6700(00)00035-6
  8. Grohmann K, Bothast RJ. Saccharification of corn fibre by combined treatment with dilute sulphuric acid and enzymes. Proc Biochem 1997;32:405-15. https://doi.org/10.1016/S0032-9592(96)00095-7
  9. Olsson L, Hahn-Hagerdal B. Fermentative performance of bacteria and yeasts in lignocellulose hydrolysates. Proc Biochem 1993;28:249-57. https://doi.org/10.1016/0032-9592(93)80041-E
  10. Fan LT, Lee YH, Gharpuray MM. The nature of lignocellulosics and their pretreatments for enzymatic hydrolysis. Adv Biochem Eng Biotechnol 1982;23:157-87.
  11. Torget R, Walter P, Himmel M, Grohmann K. Dilute-acid pretreatment of corn residues and short-rotation woody crops. Appl Biochem Biotechnol 1991;28/29:75-86.
  12. Larsson S, Palmqvist E, Hahn-Hagerdal B, Tengborg C, Stenberg K, Zacchi G, Nilvebrant NO. The generation of fermentation inhibitors during dilute acid hydrolysis of softwood. Enzyme Microb Technol 1999;24:151-9. https://doi.org/10.1016/S0141-0229(98)00101-X
  13. Yu J, Wang JP. Metabolic flux modeling of detoxification of acetic acid by Ralstonia eutropha at slightly alkaline pH levels. Biotechnol Bioeng 2001;73:458-64. https://doi.org/10.1002/bit.1080
  14. Aebersold R. Constellations in a cellular universe. Nature 2003;422:115-6. https://doi.org/10.1038/422115a
  15. Lee SE, Li QX, Yu J. Proteomic examination of Ralstonia eutropha in cellular responses to formic acid. Proteomics 2006;6:4259-68. https://doi.org/10.1002/pmic.200500824
  16. Bardwell L, Cook JG, Chang EC, Cairns BR, Thorner J. Signaling in the yeast pheromone response pathway: specific and high-affinity interaction of the mitogen-activated protein (MAP) kinases Kss1 and Fus3 with the upstream MAP kinase kinase Ste7. Mol Cell Biol 1996;16:3637-50. https://doi.org/10.1128/MCB.16.7.3637
  17. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-5. https://doi.org/10.1038/227680a0
  18. Berndt P, Hobohm U, Langen H. Reliable automatic protein identification from matrix-assisted laser desorption/ionization mass spectrometric peptide fingerprints. Eletrophoresis 1999;20:3521-6. https://doi.org/10.1002/(SICI)1522-2683(19991201)20:18<3521::AID-ELPS3521>3.0.CO;2-8
  19. Faye G, Kujawa C, Fukuhara H. Physical and genetic organization of petite and grande yeast mitochondrial DNA. IV. In vivo transcription products of mitochondrial DNA and localization of 23 S ribosomal RNA in petite mutants of Saccharomyces cerevisiae. J Mol Biol 1974;88:185-203. https://doi.org/10.1016/0022-2836(74)90304-0
  20. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with Folin phenol reagent. J Biol Chem 1951;193:265-75.
  21. Smith IK, Vierheller TL, Thorne CA. Assay of glutathione reductase in crude tissue homogenates using 5,5'-dithiobis(2-nitrobenzoic acid). Anal Biochem 1988;175:408-13. https://doi.org/10.1016/0003-2697(88)90564-7
  22. Maeda T, Wurgler-Murphy SM, Saito H. A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature 1994;369:242-5. https://doi.org/10.1038/369242a0
  23. Buck V, Quinn J, Soto Pino T, Martin H, Saldanha J, Makino K, Morgan BA, Millar JB. Peroxide sensors for the fission yeast stress-activated mitogen-activated protein kinase pathway. Mol Biol Cell 2001;12:407-19. https://doi.org/10.1091/mbc.12.2.407
  24. Stone EM, Pillus L. Activation of an MAP kinase cascade leads to Sir3p hyperphosphorylation and strengthens transcriptional silencing. J Cell Biol 1996;135:571-83. https://doi.org/10.1083/jcb.135.3.571
  25. Abbas-Terki T, Donze O, Picard D. The molecular chaperone Cdc37 is required for Ste11 function and pheromoneinduced cell cycle arrest. FEBS Lett 2000;467:1111-6.
  26. Brockerhoff SE, Stevens RC, Davis TN. The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth is Saccharomyces cerevisiae. J Cell Biol 1994;124:315-23. https://doi.org/10.1083/jcb.124.3.315
  27. Stahopoulos-Gerontides A, Guo JJ, Cyert MS. Yeast calcineurin regulates nuclear localization of the Crz1p transcription factor through dephosphorylation. Genes Dev 1999;13:798-803. https://doi.org/10.1101/gad.13.7.798
  28. Spector MS, Raff A, DeSilva H, Lee K, Osley MA. Hir1p and Hir2p function as transcriptional corepressors to regulate histone gene transcription in the Saccharomyces cerevisiae cell cycle. Mol Cell Biol 1997;17:545-52. https://doi.org/10.1128/MCB.17.2.545
  29. Peterson CL, Herskowitz I. Characterization of the yeast SWI1, SWI2, and SWI3 genes, which encode a global activator of transcription. Cell 1992;68:573-83. https://doi.org/10.1016/0092-8674(92)90192-F

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