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A small heat shock protein from Leuconostoc oenos induced by multiple stresses and during stationary growth phase

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Abstract
In Leuconostoc oenos, a malolactic bacterium, the synthesis of a stress protein called LO18 with an apparent molecular mass of 18 kDa was greatly induced after heat (42 degrees C), acid (pH 3) or ethanolic (12% (v/v)) shocks. Moreover, the LO18 protein synthesis was induced in stationary growth phase and was detected for a long time (30 h) during this growth phase. Significant identity was found between the N-terminal parts of the LO18 protein and the Hsp18 from Clostridium acetobutylicum suggesting that LO18 protein belongs to the family of small heat shock proteins conserved in prokaryotic and eukaryotic cells.
Keywords
ZYMOMONAS-MOBILIS, AERUGINOSA ALKALINE PROTEASE, ESCHERICHIA-COLI, ALPHA-CRYSTALLIN, CHAPERONES, SECRETION, CLONING, GENE, WINE

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Chicago
Guzzo, J, F Delmas, F Pierre, MP Jobin, Bart Samyn, Jozef Van Beeumen, JF Cavin, and C Diviès. 1997. “A Small Heat Shock Protein from Leuconostoc Oenos Induced by Multiple Stresses and During Stationary Growth Phase.” Letters in Applied Microbiology 24 (5): 393–396.
APA
Guzzo, J., Delmas, F., Pierre, F., Jobin, M., Samyn, B., Van Beeumen, J., Cavin, J., et al. (1997). A small heat shock protein from Leuconostoc oenos induced by multiple stresses and during stationary growth phase. LETTERS IN APPLIED MICROBIOLOGY, 24(5), 393–396.
Vancouver
1.
Guzzo J, Delmas F, Pierre F, Jobin M, Samyn B, Van Beeumen J, et al. A small heat shock protein from Leuconostoc oenos induced by multiple stresses and during stationary growth phase. LETTERS IN APPLIED MICROBIOLOGY. 1997;24(5):393–6.
MLA
Guzzo, J, F Delmas, F Pierre, et al. “A Small Heat Shock Protein from Leuconostoc Oenos Induced by Multiple Stresses and During Stationary Growth Phase.” LETTERS IN APPLIED MICROBIOLOGY 24.5 (1997): 393–396. Print.
@article{183395,
  abstract     = {In Leuconostoc oenos, a malolactic bacterium, the synthesis of a stress protein called LO18 with an apparent molecular mass of 18 kDa was greatly induced after heat (42 degrees C), acid (pH 3) or ethanolic (12\% (v/v)) shocks. Moreover, the LO18 protein synthesis was induced in stationary growth phase and was detected for a long time (30 h) during this growth phase. Significant identity was found between the N-terminal parts of the LO18 protein and the Hsp18 from Clostridium acetobutylicum suggesting that LO18 protein belongs to the family of small heat shock proteins conserved in prokaryotic and eukaryotic cells.},
  author       = {Guzzo, J and Delmas, F and Pierre, F and Jobin, MP and Samyn, Bart and Van Beeumen, Jozef and Cavin, JF and Divi{\`e}s, C},
  issn         = {0266-8254},
  journal      = {LETTERS IN APPLIED MICROBIOLOGY},
  keyword      = {ZYMOMONAS-MOBILIS,AERUGINOSA ALKALINE PROTEASE,ESCHERICHIA-COLI,ALPHA-CRYSTALLIN,CHAPERONES,SECRETION,CLONING,GENE,WINE},
  language     = {eng},
  number       = {5},
  pages        = {393--396},
  title        = {A small heat shock protein from Leuconostoc oenos induced by multiple stresses and during stationary growth phase},
  url          = {http://dx.doi.org/10.1046/j.1472-765X.1997.00042.x},
  volume       = {24},
  year         = {1997},
}

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