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Indian Journal of Agricultural Research

Studies of heat shock protein response isolated from zoom land soil bacterium (Pseudomonas spp.) 

DOI: 10.18805/ijare.v50i4.11251    | Article Id: A-211 | Page : 303-310
Citation :- Studies of heat shock protein response isolated from zoomland soil bacterium (Pseudomonas spp.) .Indian Journal of Agricultural Research.2016.(50):303-310

Lolo Wal Marzan*, Tafazzal Hossain, Yasmin Akter, Md. Amzad Hossain and Md. Arifuzzaman1

lmarzancu@yahoo.com
Address :

Department of Genetic Engineering and Biotechnology, Faculty of Biological Sciences, University of Chittagong, Chittagong- 4331, Bangladesh.

Submitted Date : 23-12-2015
Accepted Date : 3-06-2016
First Online:

Abstract

Expression of heat shock proteins (Hsps) synthesized by bacterium (Pseudomonas spp.) during stress condition (elevated temperature) is identified and studied their association in adaptation to environmental extremes. Collection, screening, isolation and identification of zoom land soil bacterium were carried out by growing bacterial cells on selective Agar Cetrimide media. Optimization of culture conditions (incubation time and temperature) for the maximum production of cell (Dry Cell Weight) also considered for the identified organism (Pseudomonas spp.) in LB media during micro-aerobic batch culture; where maximum cell growth was found 1.80 gm/L at 10 hours incubation period and 37°C incubation temperature, while rpm was 120. Subsequently, bacterial cell was grown in LB media for 6 hours at 37°C and 120 rpm into shaking incubator, then incubated for 2 hours, where maximum cell growth was observed 2.38 ± 0.06 gm/L during elevated temperature (50°C), stimulated by heat shock proteins. Then different intracellular and extracellular soluble protein extraction, purification was attempted from soil bacterium by centrifugation, sonication, repeated freezing and thawing. SDS-PAGE was performed for the separation of heat shock protein, where protein bands intensity 90, 84, 70 and 45 kDa were found according to their molecular weight. Pseudomonas spp. can produce heat shock protein during harsh condition which can help them to survive by effective adaptation mediated by universal regulatory mechanisms affecting several pathways. Hsps are expected to play a significant role to conferring tolerance in response to changes in high temperature. They are also responsible for survival of bacterial cells and increasing soil fertility which associated with virulence. So, this study will help to understand the impact of soil microorganisms to revive the soil fertility though people burn their paddy fields after harvesting in zoom areas of Bangladesh. 

Keywords

Adaptation Heat shock protein Pseudomonas spp. Stress condition Zoom land.

References

  1. Borggaard, O. K., Gafur, A. and Petersen, L. (2003). Sustainability appraisal of shifting cultivation in the Chittagong Hill Tracts of Bangladesh. AMBIO: A journal of the Human Environment, 32: 118-123. 
  2. Cheng, M. Y., Hartl, F.U., Martin, J., Pollock, R. A., Kalousek, F., Neupert, W. and Horwich, A. (1989). Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature(6208), 585-674. 
  3. Chiang, H.L., Plant, C. and Dice, J. (1989). A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science, 246: 382-385. 
  4. Chirico, W. J., Waters, M. G. and Blobel, G. (1988). 70K heat shock related proteins stimulate protein translocation into microsomes. Nature, 332: 805-810. 
  5. Choresh, O., Ron, E. and Loya, Y. (2001). The 60-kDa heat shock protein (HSP60) of the sea anemone Anemonia viridis: a potential early warning system for environmental changes. Marine Biotechnology, 3: 501-508. 
  6. Craig, E. A. and Gross, C. A. (1991). Is hsp70 the cellular thermometer? Trends in biochemical sciences, 16: 135-140. 
  7. De Maio, A. (1999). Heat shock proteins: facts, thoughts, and dreams. Shock, 11: 1-12. 
  8. Devi, M. C. and Kumar, M. S. (2012). Production, Optimization and Partial purification of Cellulase by Aspergillus niger fermented with paper and timber sawmill industrial wastes. Journal of Microbiology and Biotechnology Research, 2: 120-128. 
  9. Dinesh, S., Grundmann, H., Pitt, T. and Römling, U. (2003). European wide distribution of Pseudomonas aeruginosa clone C. Clinical microbiology and infection, 9: 1228-1233. 
  10. Euzeby, J. P. (1997). List of Bacterial Names with Standing in Nomenclature: a folder available on the Internet. International Journal of Systematic Bacteriology, 47: 590-592. 
  11. Fearnside, P. M. (2000). Global warming and tropical land-use change: greenhouse gas emissions from biomass burning, decomposition and soils in forest conversion, shifting cultivation and secondary vegetation. Climatic change, 46: 115-158. 
  12. Jakob, U., Gaestel, M., Engel, K. and Buchner, J. (1993). Small heat shock proteins are molecular chaperones. Journal of Biological Chemistry, 268: 1517-1520. 
  13. Kümmerer, K. (2004). Resistance in the environment. Journal of Antimicrobial Chemotherapy, 54: 311-320. 
  14. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685. 
  15. Lindquist, S. (1986). The heat-shock response. Annual Review of Biochemistry, 55: 1151-1191. 
  16. Lowbury, E. and Collins, A. (1955). The use of a new cetrimide product in a selective medium for Pseudomonas pyocyanea. Journal of Clinical Pathology, 8: 47. 
  17. Nam, I.-H., Chang, Y.-S., Hong, H.-B. and Lee, Y.-E. (2003). A novel catabolic activity of Pseudomonas veronii in biotransformation of pentachlorophenol. Applied Microbiology and Biotechnology, 62: 284-290. 
  18. Parsell, D. and Lindquist, S. (1993). The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annual Review of Genetics, 27: 437-496. 
  19. Peng, L. and Shimizu, K. (2006). Effect of fadR gene knockout on the metabolism of Escherichia coli based on analyses of protein expressions, enzyme activities and intracellular metabolite concentrations. Enzyme and Microbial Technology, 38: 512-520. 
  20. Pratt, W. B. and Toft, D. O. (1997). Steroid receptor interactions with heat shock protein and immunophilin chaperones 1. Endocrine Reviews, 18: 306-360. 
  21. Raboy, B., Sharon, G., Parag, H., Shochat, Y. and Kulka, R. (1990). Effect of stress on protein degradation: role of the ubiquitin system. Acta Biologica Hungarica, 42: 3-20. 
  22. Schlesinger, M. J. (1990). Heat shock proteins. J Biol Chem, 265: 12111-12114. 
  23. Scroggins, B. T., Robzyk, K., Wang, D., Marcu, M. G., Tsutsumi, S., Beebe, K., . . . Karnitz, L. (2007). An acetylation site in the middle domain of Hsp90 regulates chaperone function. Molecular cell, 25: 151-159. 
  24. Segal, G. and Ron, E. Z. (2006). Heat shock transcription of the groESL operon of Agrobacterium tumefaciens may involve a hairpin-loop structure. Journal of Bacteriology, 175: 3083-3088. 
  25. Sriramulu, D. D., Lünsdorf, H., Lam, J. S. and Römling, U. (2005). Microcolony formation: a novel biofilm model of Pseudomonas aeruginosa for the cystic fibrosis lung. Journal of Medical Microbiology, 54: 667-676. 
  26. Walter, S. and Buchner, J. (2002). Molecular chaperones—cellular machines for protein folding. Angewandte Chemie International Edition, 41: 1098-1113. 
  27. Wehmhöner, D., Häussler, S., Tümmler, B., Jänsch, L., Bredenbruch, F., Wehland, J. and Steinmetz, I. (2003). Inter-and intraclonal diversity of the Pseudomonas aeruginosa proteome manifests within the secretome. Journal of Bacteriology, 185: 5807-5814. 
  28. Wu, C. (1995). Heat shock transcription factors: structure and regulation. Annual Review of Cell and Developmental Biology, 11: 441-469. 
  29. Zhao, L. and Jones, W. (2012). Expression of heat shock protein genes in insect stress responses. Invertebrate Surviv. J, 9: 93-101.

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