The groESL operon of the halophilic lactic acid bacterium Tetragenococcus halophila

The groESL operon of the halophilic lactic acid bacterium Tetragenococcus halophila was cloned by a PCR-based method. The molecular masses of GroES and GroEL proteins were calculated to be 10,153 and 56,893 Da, respectively. The amount of groESL mRNA was increased 3.8-fold by heat shock (45degC), an...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2002-05, Vol.66 (5), p.1176-1180
Hauptverfasser:	Fukuda, D. (Kyushu Univ., Fukuoka (Japan)), Watanabe, M, Aso, Y, Sonomoto, K, Ishizaki, A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacterial Proteins - genetics Bacteriology Base Sequence Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Chaperonins - genetics CIRCE DNA, Bacterial Fundamental and applied biological sciences. Psychology GENES Genetics groESL operon halophile HALOPHYTES heat shock protein HEAT STRESS LACTIC ACID BACTERIA Lactobacillaceae - genetics Microbiology Mission oriented research MOLECULAR CLONING Molecular Sequence Data MOLECULAR WEIGHT NUCLEOTIDE SEQUENCE Operon PCR PROTEINS Tetragenococcus
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Zusammenfassung:	The groESL operon of the halophilic lactic acid bacterium Tetragenococcus halophila was cloned by a PCR-based method. The molecular masses of GroES and GroEL proteins were calculated to be 10,153 and 56,893 Da, respectively. The amount of groESL mRNA was increased 3.8-fold by heat shock (45degC), and 4-fold by high NaCl (3-4 M). The Bacillus subtilis s**A-like constitutive promoter existed in front of groES, and was used under both normal and stress (heat shock and high salinity) conditions.
ISSN:	0916-8451 1347-6947
DOI:	10.1271/bbb.66.1176