Isolation and characterization of a cytosolic aldehyde dehydrogenase-encoding cDNA from mouse liver

Betaine aldehyde dehydrogenase (BADH) catalyzes the last step in the synthesis of the glycine betaine from choline. The BADH gene from turfgrass Ophiopogon japonicus has not been reported. In this study, we first isolated the full length cDNA of betaine aldehyde dehydrogenase gene (OjBADH) from O. japonicus using Reverse Transcriptase- Polymerase Chain Reaction (RT-PCR) and Rapid Amplification of cDNA Ends (RACE) techniques. The OjBADH gene (GenBank accession number: DQ645888) has 1785 nucleotides with the 5’ untranscribed region (UTR) of 63 nucleotides, 3’ UTR of 219 nucleotides, and an open reading frame of 1503 nucleotides. This gene encodes a polypeptide of 500 amino acids. It shares a high homology with BADH genes of other Chenopodiaceae species. The putative protein includes a conservative region of phosphofructokinase, aldehyde dehydrogenase, and glutamy phosphoric acid reductase. Overexpression of OjBADH in transgenic tobacco plants demonstrated 2-2.5 folds increase of glycine betaine content and 60- 85% increase of survival rate under salt tolerance. These results suggested that the O. japonicus BADH gene may be used to engineer plants for salt stress tolerance.

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Isolation and characterization of an hydroxykynureninase from homogenates of adult mouse liver

Biochemical and Biophysical Research Communications ◽

10.1016/0006-291x(73)91387-9 ◽

1973 ◽

Vol 51 (3) ◽

pp. 813-818 ◽

Cited By ~ 9

Author(s):

C.E. McDermott ◽

D.A. Casciano ◽

F.H. Gaertner

Keyword(s):

Mouse Liver ◽

Adult Mouse ◽

Isolation And Characterization ◽

Adult Mouse Liver

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Isolation and Characterization of Human Liver Aldehyde Dehydrogenase

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)93153-4 ◽

1968 ◽

Vol 243 (24) ◽

pp. 6402-6408

Author(s):

R J Kraemer ◽

R A Deitrich

Keyword(s):

Aldehyde Dehydrogenase ◽

Human Liver ◽

Isolation And Characterization ◽

Liver Aldehyde Dehydrogenase

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Isolation and characterization of two mouse Pi-class glutathione S-transferase genes

Biochemical Journal ◽

10.1042/bj2980385 ◽

1994 ◽

Vol 298 (2) ◽

pp. 385-390 ◽

Cited By ~ 50

Author(s):

T K Bammler ◽

C A D Smith ◽

C R Wolf

Keyword(s):

Mouse Liver ◽

Peptide Sequence ◽

Tata Box ◽

Sequence Motif ◽

Glutathione S Transferase ◽

Coding Regions ◽

Isolation And Characterization ◽

Glutathione S Transferases ◽

Responsive Element

Pi-class glutathione S-transferases (GSTs) play an important role in the detoxification of chemical toxins and mutagens and are implicated in neoplastic development and drug resistance. In all species characterized to date, only one functional Pi-class GST gene has been described. In this report we have identified two actively transcribed murine Pi-class GST genes, Gst p-1 and Gst p-2. The coding regions of Gst p-1 and the mouse Pi-class GST cDNA (GST-II) reported by Hatayama, Satoh and Satoh (1990) (Nucleic Acids Res. 18, 4606) are identical, whereas Gst p-2 encodes a protein that has not been described previously. The two genes are approximately 3 kb long and contain seven exons interrupted by six introns. In addition to a TATA box and a sequence motif matching the phorbol-ester-responsive element, the promoters of Gst p-1 and Gst p-2 exhibit one and two G+C boxes (GGGCGG) respectively. The cDNAs of the two genes were isolated from total liver RNA using reverse PCR. The peptide sequence deduced from the cDNAs share 97% identity and differ in six amino acids. Both genes are transcribed at significantly higher levels in male mouse liver than in female, and Gst p-1 mRNA is more abundant in both sexes than Gst p-2.

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