Molecular cloning and characterization of the guinea pig cholinephosphotransferase gene
| Autor: | Salil K. Das, Asit K Chakraborty |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Pseudogene
Molecular Sequence Data Biophysics Sequence Homology Biology Molecular cloning Biochemistry Species Specificity Sequence Analysis Protein Complementary DNA Animals Humans Amino Acid Sequence Cloning Molecular Molecular Biology Gene Genomic organization chemistry.chemical_classification Base Sequence Oligonucleotide Cell Biology Molecular biology Recombinant Proteins Amino acid Molecular Weight Restriction enzyme chemistry Diacylglycerol Cholinephosphotransferase Sequence Alignment |
| Zdroj: | Biochemical and biophysical research communications. 312(4) |
| ISSN: | 0006-291X |
| Popis: | Cholinephosphotransferase (CPT), the terminal enzyme in the de novo synthesis of phosphatidylcholine (PC), has an important role in regulating the acyl group of PC in mammalian cells. A 593 bp cDNA coding for the 3 ′ -end of the CPT gene has been cloned from guinea pig liver using degenerative oligos based on the human CPT gene. It has 85% amino acid homology with the human CPT enzyme and amino acid variations were found to cluster at few points. Restriction enzyme polymorphisms were found particularly with respect to Bam HI and Nco I. Hydrophobic and helix plot analysis of the sequence shows a similar pattern to human counterpart except for amino acid residues 142–179 and 173–179. PCR analysis suggested that a predominant pseudogene may be present in guinea pig and also the intronic sequences were much shorter when compared to the human CPT gene. We are the first to report on the C-terminal 195 amino acid residues of the CPT gene from any animal species alike in many aspects of cellular metabolism. The probable differences in genomic organization and its expression in different cancer cells have been discussed here having CPT as an important target for cancer drug development. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect