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 (45 degrees C), and 4-fold by high NaCl (3-4 M). The Bacillus subtilis sigmaA-like constitutive promoter existed in front of groES, and was used under both normal and stress (heat shock and high salinity) conditions.
Fukuda
Daisuke
D
Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University, Fukuoka, Japan.
Watanabe
Maki
M
Aso
Yuji
Y
Sonomoto
Kenji
K
Ishizaki
Ayaaki
A
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001483:Base Sequence; D018833:Chaperonins / Q000235:genetics*; D004269:DNA, Bacterial; D007777:Lactobacillaceae / Q000235:genetics*; D008969:Molecular Sequence Data; D009876:Operon
D001426:Bacterial Proteins; D004269:DNA, Bacterial; C097970:GroESL protein, Bacteria; D018833:Chaperonins