Cloning and characterization of a novel glutathione transferase gene from Penicillium chrysogenum.
- Author:
Yuan ZHANG
1
;
Fu-Qiang WANG
;
Gui-Zhen ZHENG
;
Meng DAI
;
Jing LIU
;
Ying ZHAO
;
Zhi-Hong REN
;
Bao-Hua ZHAO
;
Qian JIA
Author Information
1. College of Life Sciences, Hebei Normal University, Shijiazhuang 050016, China.
- Publication Type:Journal Article
- MeSH:
Catalysis;
Cloning, Molecular;
Escherichia coli;
genetics;
metabolism;
Fungal Proteins;
genetics;
metabolism;
Genes, Bacterial;
genetics;
Glutathione Transferase;
genetics;
metabolism;
Open Reading Frames;
Penicillium chrysogenum;
enzymology;
genetics;
Recombinant Proteins;
biosynthesis;
genetics;
Sequence Analysis, Protein
- From:
Chinese Journal of Biotechnology
2007;23(4):618-622
- CountryChina
- Language:Chinese
-
Abstract:
Glutathione transferases (GSTs) are a family of multifunctional proteins that mainly catalyze the conjugation of intracellular glutathione (GSH) to a wide variety of endogenous and exogenous electrophilic compounds. GSTs play important roles in stress tolerance and in the detoxification metabolism in organisms. A novel GST gene, Pc gstB, was cloned from penicillin producing fungus Penicillium chrysogenum using RT-PCR. The open reading frame (ORF) of Pc gstB was 651 bp and encoded a peptide of 216 residues. The deduced amino acids sequence had conserved GST domain and showed 65% identity to the characterized Aspergillus fumigutus gstB. The entire ORF of Pc gstB was inserted into vector pTrc99A and transformed into Escherichia coli DH5alpha. Recombinant PcGstB was overexpressed and its GST activity toward substrate 1-chloro-2,4-dinitrobenzene (CDNB) was validated.
