- Volume 21 Issue 11
DOI QR Code
Cloning and Sequence Analysis of Glyceraldehyde-3-Phosphate Dehydrogenase Gene in Yak
- Li, Sheng-Wei (College of Life Sciences and Technology, Southwest University for Nationalities) ;
- Jiang, Ming-Feng (College of Life Sciences and Technology, Southwest University for Nationalities) ;
- Liu, Yong-Tao (College of Life Sciences and Technology, Southwest University for Nationalities) ;
- Yang, Tu-Feng (College of Life Sciences and Technology, Southwest University for Nationalities) ;
- Wang, Yong (College of Life Sciences and Technology, Southwest University for Nationalities) ;
- Zhong, Jin-Cheng (College of Life Sciences and Technology, Southwest University for Nationalities)
- Received : 2008.04.22
- Accepted : 2008.07.18
- Published : 2008.11.01
In order to study the biological function of gapdh gene in yak, and prove whether the gapdh gene was a useful intra-reference gene that can be given an important role in molecular biology research of yak, the cDNA sequence encoding glyceraldehyde-3-phosphate dehydrogenase from yak was cloned by the RT-PCR method using gene specific PCR primers. The sequence results indicated that the cloned cDNA fragment (1,008 bp) contained a 1,002 bp open reading frame, encoding 333 amino acids (AAs) with a molecular mass of 35.753 kDa. The deduced amino acids sequence showed a high level of sequence identity to Bos Taurus (99.70%), Xenopus laevis (94.29%), Homo sapiens (97.01%), Mus musculus (97.90%) and Sus scrofa (98.20%). The expression of yak's gapdh gene in heart, spleen, kidney and brain tissues was also detected; the results showed that the gapdh gene was expressed in all these tissues. Further analysis of yak GAPDH amino acid sequence implied that it contained a complete glyceraldehyde-3-phosphate dehydrogenase active site (ASCTTNCL) which ranged from 148 to 155 amino acid residues. It also contained two conserved domains, a NAD binding domain in its N-terminal and a complete catalytic domain of sugar transport in its C-terminal. The phylogenetic analysis showed that yak and Bos taurus were the closest species. The prediction of secondary structures indicated that GAPDH of yak had a similar secondary structure to other isolated GAPDH. The results of this study suggested that the gapdh gene of yak was similar to other species and could be used as the intra-reference to analyze the expression of other genes in yak.
Yak;Glyceraldehyde-3-Phosphate Dehydrogenase gene;Cloning;Housekeeping Gene
- Vila, M. R., A. Nicolas and J. Morote. 2000. Increased glyceraldehyde-3-phosphate dehydrogenase expression in renal cell carcinoma identified by RNA-based, arbitrarily primed polymerase chain reaction. Cancer. 89(1):152-164. https://doi.org/10.1002/1097-0142(20000701)89:1<152::AID-CNCR20>3.0.CO;2-T
- Yamagata, M., M. Mori, N. A. Begum, K. Shibuta, K. Shimoda and G. F. Barnard. 1998. GIyceraldehyde-3-phosphate Dehydrogenase mRNA expression in hepatocellular carcinoma. Int. J. Oncol. 12(3):677-683.
- Zang, W. Q., A. M. Fieno, R. A. Grant and T. S. Yen. 1998. Identification of glyceraldehyde-3-phosphate as a cellular protein that binds to the hepatitis B virus posttranscriptional regulatory element. Virology 248(1):46-52. https://doi.org/10.1006/viro.1998.9255
- Schek, N., B. L. Hall and O. J. Finn. 1988. Increased glyceraldehyde-3-phosphate dehydrogenase gene expression human pancreatic adenocarcinoma. Cancer. Res. 48:6354-6359.
- Singh, R. and M. R. Green. 1993. Sequence-specificity binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase. Sci. 259(5093):365-368. https://doi.org/10.1126/science.8420004
- Sirover, M. A. 1999. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Bioehlm. Biophys. Acts. 1432(2):159-184. https://doi.org/10.1016/S0167-4838(99)00119-3
- Sirover, M. A. 1997. Role of the glycolytic protein, glyceraldehydes-3-phosphate dehydrogenase, in normal cell function and in cell pathology. J. Cel. Bio. 66:133-140. https://doi.org/10.1002/(SICI)1097-4644(19970801)66:2<133::AID-JCB1>3.0.CO;2-R
- Tisdale, E. J. 2002. Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway. J. Biol. Chem. 277(5):3334-3341. https://doi.org/10.1074/jbc.M109744200
- Miller, D. J., R. B. Harris and Cui-Quan Cai. 1994. Wild yak and their consercation in the Tibetan Plateau. Proceedings of the first international congress on yak. Journal of Gansu Agricultural University (Special issue June 1994). pp. 27-35.
- Robbins, A. R., R. D. Ward and C. Oliver. 1995. A mutation in glyceraldehydes-3-phosphate dehydrogenase alters endocytosis in CHO cells. J. Cel. Biol. 130(5):1093-1094. https://doi.org/10.1083/jcb.130.5.1093
- Lee, S. H., E. W. Park, Y. M. Cho, S. K. Kim, J. H. Lee, J. T. Jeon, C. S. Lee, S. K. Im, S. J. Oh, J. M. Thompson and D. Yoon. 2007. Identification of differentially expressed genes related to intramuscular fat development in the early and late fattening stages of hanwoo steers. J. Biochem. Mol. Biol. 30;40(5):757-64. https://doi.org/10.5483/BMBRep.2007.40.5.757
- Maglott, D, J. Ostell, K. D. Pruitt and T. Tatusova. 2007. Entrez Gene: gene-centered information at NCBI. Nucleic Acids Res. 35:26-31.
- Martin, W., H. Brinkmann, C. Savonna and R. Cerff. 1993. Evidence for a chimeric nature of nuclear genomes: eubacterial origin of eukaryotic glyceraldehyde-3-phosphate dehydrogenasegenes. Proc. Natn. Acad. Sci. USA. 90:8692-8696. https://doi.org/10.1073/pnas.90.18.8692
- Hocquette, J. F., B. Graulet C. Castiglia-Delavaud, F. Bornes, N. Lepetit and P. Ferre. 1996. Insulin-sensitive glucose transporter transcript levels in calf muscles assessed with a bovine GLUT4 cDNA fragment. Int. J. Biochem. Cell Biol. 28(7):795-806. https://doi.org/10.1016/1357-2725(96)00013-1
- Katherine, M. S., R. M. Nasima, C. W. James and A. S. Michael. 1992. Proliferative dependent regulation of the glyceraldehyde-3-phosphate dehydrogenase/uracil DNA glycosylase gene in human cells. Carcinogenesis 13(11):21-27.
- Kim, H. H., M. B. Seol, D. H. Jeon, S. S. Sun, K. H. Kim, Y. J. Choi and M. G. Baik. 2001. Cloning and expression of lactate dehydrogenase H chain gene in adipose tissues of Korean cattle. Asian-Aust. J. Anim. Sci. 14(12):1670-1674. https://doi.org/10.5713/ajas.2001.1670
- Gerald, W., J. L. Han and R. J. Long. 2003. The yak. Published by the regional office for Asia and the pacific food and agriculture organization of the united nationa, Bangkok, Thailand.
- Gianni, C., A. Giovanna, F. Myriam, G. Gastone and Nussdorfer. 2005. Similar sequence-free amplification of human glyceraldehydes-3-phosphate dehydrogenase for real time RT-PCR applications. Mol. Cell. Probes. 19:181-186. https://doi.org/10.1016/j.mcp.2004.11.004
- Gong, Y., L. Cui and G. Y. Minuk. 1996. Comparison of glyceraldehyde-3-phosphate dehydrogenase and 28s-ribosomal RNA gene expresslon in human hepatocellular carcinoma. Hepatology 23(4):734-737. https://doi.org/10.1002/hep.510230413
- Haque, B. U., R. A. Belecheanu, R. J. Barson, K. S. Pawar, F. Revillion, V. Pawlowski, L. Hornez and J. P. Peyrat. 2000. Glyceraldehyde-3-phosphate dehydrogenase gene expression in human breast cancer. Eur. J. Cancer. 36(8):1038-1042. https://doi.org/10.1016/S0959-8049(00)00051-4
- Altschul, S. F., T. L. Madden, A. A. Schaffer, J. Zhang, Z. Zhang, W. Miller and D. J. Lipman. 1997. Gapped BLAST and PSIBLAST: a new generation of protein database search programs. Nucleic Acids Res. 25(17):3389-3402. https://doi.org/10.1093/nar/25.17.3389
- Berry, M. D. and A. A. Boulton. 2000. Glyceraldehyde-3-phosphate dehydrogenase and apoptosis. J. Neu. Res. 60:150-154. https://doi.org/10.1002/(SICI)1097-4547(20000415)60:2<150::AID-JNR3>3.0.CO;2-4
- Engel, M., M. Seifert, B. Theisinger, U. Seyfert and C. Welter. 1998. Glyceraldehyde-3-phosphate dehydrogenase and Nm23H1/nucleoside diphosphate kinase A: two old enzymes combine for the novel Nm23 protein phosphotransferase function. J. Biol. Chem. 273(32):20058-20065. https://doi.org/10.1074/jbc.273.32.20058
- Mazzola, J. L. and M. A. Sirover. 2003. Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of it s glycolytic function. Biochimica and Biophysica Acta, 16(22):50-56.
- Viscogliosi, E. and M. M. Ller. 1998. Phylogenetic relationships of the glycolytic enzyme, glyceraldehyde-3-phosphatedehydrogenase, fromparabasalid flagellates. J. Mol. Evol. 47:190-199. https://doi.org/10.1007/PL00006376