Research Article
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Evaluation of Proteins Released to Medium in Yeast-Bacteria Co-culture System

Year 2023, Volume: 9 Issue: 2, 488 - 498, 30.06.2023
https://doi.org/10.28979/jarnas.1196962

Abstract

Cultivation of microorganisms in ideal laboratory conditions seperates them from their natural conditions and isolates them from their microbial world, especially from their competitors. With traditional pure culture-oriented cultuvation techniques, interactions mediated by small molecules are not taken into account, resulting in the precise nature of the interactions being largely unknown. Co-culture systems are systems in which two or more different cell populations are grown together. In this way, studies on natural interactions between populations can be made and synthetic interactions that are not observed in nature can be provided. With these systems, natural product discovery, microbial ecology, evolution and pathogenesis studies are carried out. In addition, co-culture systems are also used in industrial, environmental and medical studies. In this study, the wild strain of Schizosaccharomyces pombe and the DH5α strain of Escherichia coli were grown in their own specific media, then cultured for 48 hours and 72 hours by cultivating in media containing 0,1% glucose with different cell number, and finally the differentiation in the proteins released by the cells into the medium was observed in SDS polyacrylamide gels. Different from the control conditions, new protein bands that emerged under the co-culture conditions were detected and two of these bands were analyzed by mass spectrometry (MS). While 6 of differentaited proteins were released by S.pombe, 257 proteins matched with E.coli proteom. These proteins are; Various carbohydrate-binding proteins, membrane proteins involved in the identification of various signaling molecules and antibiotics, and other proteins involved in various cellular processes.

Supporting Institution

İstanbul Üniversitesi Bilimsel Araştırma Projeleri Birimi

Project Number

33600

Thanks

This study was supported by Istanbul University Scientific Research Projects Unit (BAP) with project number 33600. We thank BAP for their support.

References

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Year 2023, Volume: 9 Issue: 2, 488 - 498, 30.06.2023
https://doi.org/10.28979/jarnas.1196962

Abstract

Project Number

33600

References

  • Ackerley, D. F., Gonzalez, C. F., Park, C. H., Blake, R., 2nd, Keyhan, M., & Matin, A. (2004). Chromate-reducing properties of soluble flavoproteins from Pseudomonas putida and Escherichia coli. Applied and environmental microbiology, 70(2), 873–882. https://doi.org/10.1128/AEM.70.2.873-882.2004
  • Almirón, M., Link, A. J., Furlong, D., & Kolter, R. (1992). A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes & development, 6(12B), 2646–2654. https://doi.org/10.1101/gad.6.12b.2646
  • Anderson, G. G., Palermo, J. J., Schilling, J. D., Roth, R., Heuser, J., & Hultgren, S. J. (2003). Intracellular bacterial biofilm-like pods in urinary tract infections. Science (New York, N.Y.), 301(5629), 105–107. https://doi.org/10.1126/science.1084550
  • Atlas, R.M., Bartha, R. (1998), Microbial ecology: fundamentals and applications, 4th ed., Addison Wesley Longman California, ISBN: 0805306552.
  • Bailey, J.E., Ollis, D.F. (1986). Biochemical engineering fundamentals, 2nd ed. McGraw-Hill, New York, ISBN: 9781138748071.
  • Beck, C. M., Willett, J. L., Cunningham, D. A., Kim, J. J., Low, D. A., & Hayes, C. S. (2016). CdiA Effectors from Uropathogenic Escherichia coli Use Heterotrimeric Osmoporins as Receptors to Recognize Target Bacteria. PLoS pathogens, 12(10), e1005925. https://doi.org/10.1371/journal.ppat.1005925
  • Bermúdez-Humarán, L. G., Kharrat, P., Chatel, J. M., & Langella, P. (2011). Lactococci and lactobacilli as mucosal delivery vectors for therapeutic proteins and DNA vaccines. Microbial cell factories, 10 Suppl 1(Suppl 1), S4. https://doi.org/10.1186/1475-2859-10-S1-S4
  • Chai, T. J., & Foulds, J. (1977). Purification of protein A, an outer membrane component missing in Escherichia coli K-12 ompA mutants. Biochimica et biophysica acta, 493(1), 210–215. https://doi.org/10.1016/0005-2795(77)90274-4
  • Chao, L., & Levin, B. R. (1981). Structured habitats and the evolution of anticompetitor toxins in bacteria. Proceedings of the National Academy of Sciences of the United States of America, 78(10), 6324–6328. https://doi.org/10.1073/pnas.78.10.6324
  • Choi, U., & Lee, C. R. (2019). Distinct Roles of Outer Membrane Porins in Antibiotic Resistance and Membrane Integrity in Escherichia coli. Frontiers in microbiology, 10, 953. https://doi.org/10.3389/fmicb.2019.00953
  • Chaturvedi, D., & Mahalakshmi, R. (2017). Transmembrane β-barrels: Evolution, folding and energetics. Biochimica et biophysica acta. Biomembranes, 1859(12), 2467–2482. https://doi.org/10.1016/j.bbamem.2017.09.020
  • Choudhury, D., Thompson, A., Stojanoff, V., Langermann, S., Pinkner, J., Hultgren, S. J., & Knight, S. D. (1999). X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli. Science (New York, N.Y.), 285(5430), 1061–1066. https://doi.org/10.1126/science.285.5430.1061
  • Cottet, S., Corthésy-Theulaz, I., Spertini, F., & Corthésy, B. (2002). Microaerophilic conditions permit to mimic in vitro events occurring during in vivo Helicobacter pylori infection and to identify Rho/Ras-associated proteins in cellular signaling. The Journal of biological chemistry, 277(37), 33978–33986. https://doi.org/10.1074/jbc.M201726200
  • da Silva, G. P., Mack, M., & Contiero, J. (2009). Glycerol: a promising and abundant carbon source for industrial microbiology. Biotechnology advances, 27(1), 30–39. https://doi.org/10.1016/j.biotechadv.2008.07.006
  • Dam, S., Pagès, J. M., & Masi, M. (2017). Dual Regulation of the Small RNA MicC and the Quiescent Porin OmpN in Response to Antibiotic Stress in Escherichia coli. Antibiotics (Basel, Switzerland), 6(4), 33. https://doi.org/10.3390/antibiotics6040033
  • Dekoninck, K., Létoquart, J., Laguri, C., Demange, P., Bevernaegie, R., Simorre, J. P., Dehu, O., Iorga, B. I., Elias, B., Cho, S. H., & Collet, J. F. (2020). Defining the function of OmpA in the Rcs stress response. eLife, 9, e60861. https://doi.org/10.7554/eLife.60861
  • Diggle, S. P., Griffin, A. S., Campbell, G. S., & West, S. A. (2007). Cooperation and conflict in quorum-sensing bacterial populations. Nature, 450(7168), 411–414. https://doi.org/10.1038/nature06279
  • Diner, E. J., Beck, C. M., Webb, J. S., Low, D. A., & Hayes, C. S. (2012). Identification of a target cell permissive factor required for contact-dependent growth inhibition (CDI). Genes & development, 26(5), 515–525. https://doi.org/10.1101/gad.182345.111
  • Dupont, M., James, C. E., Chevalier, J., & Pagès, J. M. (2007). An early response to environmental stress involves regulation of OmpX and OmpF, two enterobacterial outer membrane pore-forming proteins. Antimicrobial agents and chemotherapy, 51(9), 3190–3198. https://doi.org/10.1128/AAC.01481-06
  • Edwards, R., Baker, H., Whittaker, M. et al. Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1-Å resolution. JBIC 3, 161–171 (1998). https://doi.org/10.1007/s007750050217
  • Egli, T., Lendenmann, U., & Snozzi, M. (1993). Kinetics of microbial growth with mixtures of carbon sources. Antonie van Leeuwenhoek, 63(3-4), 289–298. https://doi.org/10.1007/BF00871224
  • Ferenci T. (1996). Adaptation to life at micromolar nutrient levels: the regulation of Escherichia coli glucose transport by endoinduction and cAMP. FEMS microbiology reviews, 18(4), 301–317. https://doi.org/10.1111/j.1574-6976.1996.tb00246.x Foulds, J., & Chai, T. J. (1978). New major outer membrane proteins found in an Escherichia coli tolF mutant resistant to bacteriophage TuIb. Journal of bacteriology, 133(3), 1478–1483. https://doi.org/10.1128/jb.133.3.1478-1483.1978
  • Fuqua, C., & Greenberg, E. P. (2002). Listening in on bacteria: acyl-homoserine lactone signalling. Nature reviews. Molecular cell biology, 3(9), 685–695. https://doi.org/10.1038/nrm907
  • Ghai, I., Bajaj, H., Arun Bafna, J., El Damrany Hussein, H. A., Winterhalter, M., & Wagner, R. (2018). Ampicillin permeation across OmpF, the major outer-membrane channel in Escherichia coli. The Journal of biological chemistry, 293(18), 7030–7037. https://doi.org/10.1074/jbc.RA117.000705
  • Ghoul, M., & Mitri, S. (2016). The Ecology and Evolution of Microbial Competition. Trends in microbiology, 24(10), 833–845. https://doi.org/10.1016/j.tim.2016.06.011
  • Goers, L., Freemont, P., & Polizzi, K. M. (2014). Co-culture systems and technologies: taking synthetic biology to the next level. Journal of the Royal Society, Interface, 11(96), 20140065. https://doi.org/10.1098/rsif.2014.0065
  • Gonzalez, C. F., Ackerley, D. F., Lynch, S. V., & Matin, A. (2005). ChrR, a soluble quinone reductase of Pseudomonas putida that defends against H2O2. The Journal of biological chemistry, 280(24), 22590–22595. https://doi.org/10.1074/jbc.M501654200
  • González-Pérez, M. M., van Dillewijn, P., Wittich, R. M., & Ramos, J. L. (2007). Escherichia coli has multiple enzymes that attack TNT and release nitrogen for growth. Environmental microbiology, 9(6), 1535–1540. https://doi.org/10.1111/j.1462-2920.2007.01272.x
  • Gonzalez, R., Murarka, A., Dharmadi, Y., & Yazdani, S. S. (2008). A new model for the anaerobic fermentation of glycerol in enteric bacteria: trunk and auxiliary pathways in Escherichia coli. Metabolic engineering, 10(5), 234–245. https://doi.org/10.1016/j.ymben.2008.05.001
  • Griffin, A. S., West, S. A., & Buckling, A. (2004). Cooperation and competition in pathogenic bacteria. Nature, 430(7003), 1024–1027. https://doi.org/10.1038/nature02744
  • Heffernan, E. J., Wu, L., Louie, J., Okamoto, S., Fierer, J., & Guiney, D. G. (1994). Specificity of the complement resistance and cell association phenotypes encoded by the outer membrane protein genes rck from Salmonella typhimurium and ail from Yersinia enterocolitica. Infection and immunity, 62(11), 5183–5186. https://doi.org/10.1128/iai.62.11.5183-5186.1994
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There are 57 citations in total.

Details

Primary Language English
Subjects Structural Biology
Journal Section Research Article
Authors

Ayşegül Yanık 0000-0002-6989-9355

Çağatay Tarhan 0000-0001-5265-4610

Project Number 33600
Early Pub Date June 21, 2023
Publication Date June 30, 2023
Submission Date October 31, 2022
Published in Issue Year 2023 Volume: 9 Issue: 2

Cite

APA Yanık, A., & Tarhan, Ç. (2023). Evaluation of Proteins Released to Medium in Yeast-Bacteria Co-culture System. Journal of Advanced Research in Natural and Applied Sciences, 9(2), 488-498. https://doi.org/10.28979/jarnas.1196962
AMA Yanık A, Tarhan Ç. Evaluation of Proteins Released to Medium in Yeast-Bacteria Co-culture System. JARNAS. June 2023;9(2):488-498. doi:10.28979/jarnas.1196962
Chicago Yanık, Ayşegül, and Çağatay Tarhan. “Evaluation of Proteins Released to Medium in Yeast-Bacteria Co-Culture System”. Journal of Advanced Research in Natural and Applied Sciences 9, no. 2 (June 2023): 488-98. https://doi.org/10.28979/jarnas.1196962.
EndNote Yanık A, Tarhan Ç (June 1, 2023) Evaluation of Proteins Released to Medium in Yeast-Bacteria Co-culture System. Journal of Advanced Research in Natural and Applied Sciences 9 2 488–498.
IEEE A. Yanık and Ç. Tarhan, “Evaluation of Proteins Released to Medium in Yeast-Bacteria Co-culture System”, JARNAS, vol. 9, no. 2, pp. 488–498, 2023, doi: 10.28979/jarnas.1196962.
ISNAD Yanık, Ayşegül - Tarhan, Çağatay. “Evaluation of Proteins Released to Medium in Yeast-Bacteria Co-Culture System”. Journal of Advanced Research in Natural and Applied Sciences 9/2 (June 2023), 488-498. https://doi.org/10.28979/jarnas.1196962.
JAMA Yanık A, Tarhan Ç. Evaluation of Proteins Released to Medium in Yeast-Bacteria Co-culture System. JARNAS. 2023;9:488–498.
MLA Yanık, Ayşegül and Çağatay Tarhan. “Evaluation of Proteins Released to Medium in Yeast-Bacteria Co-Culture System”. Journal of Advanced Research in Natural and Applied Sciences, vol. 9, no. 2, 2023, pp. 488-9, doi:10.28979/jarnas.1196962.
Vancouver Yanık A, Tarhan Ç. Evaluation of Proteins Released to Medium in Yeast-Bacteria Co-culture System. JARNAS. 2023;9(2):488-9.


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