Chemistry: molecular biology and microbiology – Micro-organism – per se ; compositions thereof; proces of... – Bacteria or actinomycetales; media therefor
Patent
1997-09-05
1998-10-27
Elliott, George C.
Chemistry: molecular biology and microbiology
Micro-organism, per se ; compositions thereof; proces of...
Bacteria or actinomycetales; media therefor
4353201, 536 232, 536 235, 536 2431, C12N 121, C12N 1512, C12N 1570, C07H 2104
Patent
active
058277269
DESCRIPTION:
BRIEF SUMMARY
This application is a 371 of PCT/JP96/00660 filed Mar. 15, 1996.
TECHNICAL FIELD
This invention relates to a novel DNA containing the consensus sequence of a protein kinase catalytic domain. More specifically, the invention relates to a novel DNA containing a catalytic domain consensus sequence characteristics of serine/threonine kinase. The invention also relates to a plasmid containing said DNA, a transformant having said plasmid, a process for producing said DNA, and an oligonucleotide capable of specific hybridization with said DNA.
BACKGROUND ART
The studies on the mechanism of signal transduction into eukaryotic cells in response to external stimuli have seen a rapid progress in recent years.
For instance, it has been unravelled that intracellular signal transduction is accomplished by a complex kinase-cascaded signal transduction system in response to stimulation by growth factors such as a nerve growth factor (NGF) and an epidermal growth factor (EGF) and it is known that a growth factor receptor which is a kind of tyrosine kinases and an MAP kinase family which is a kind of serine/threonine kinases are both involved in the transduction mechanism (Williams, L.T. et al., Annu. Rev. Biochem., 1993, 62, 453-481; Boleu, J. B. Oncogene, 1993, 8, 2025-2031; Davis, R. J., J. Biol. Chem., 268, 1993, 14553-14556). It is also known that the phosphorylation and dephosphorylation of proteins with enzymes belonging to a cycline-dependent kinase (CDK) family which is a kind of serine/threonine kinases are involved in the regulation of cell cycles and studies on the details of the mechanism are in progress (Nurse, P., Nature, 344, 503-508, 1990; Pines, J., Trends Biochem. Sci., 19, 143-145, 1994).
In addition, an SNF1 gene is known as one of the genes believed to play an important role in the metabolism of saccharides in yeast cells.
Further in addition, it has recently been reported that an AMP activated protein kinase (AMPK) gene cloned from the rat liver shows a high level of homology in amino acid sequence to the SNF1 gene (Carling, D. et al., J. Biol. Chem., 1994, 269, 11442-11448). It is found that the AMPK inactivates enzymes such as acetyl CoA carboxylase which catalyzes the first step of fatty acid synthesis, 3-hydroxy-3-methylglutaryl CoA reductase which is a key enzyme to the biosynthesis of cholesterol and other isoprenoid compounds, and hormone-sensitive lipase in a way of phosphorylation and it is considered to be one of the important regulatory factors in lipid metabolisms including the metabolism of triglycerides or cholesterol esters (Clarke, P. R. et al., EMBO J., 1990, 9, 2439-2446). Thus, it has been suggested that the SNF1 family is heavily involved in the metabolic regulation of carbon compounds such as saccharides or lipids in eukaryotic cells.
As described above, many reports have suggested that the phosphorylation and dephosphorylation of proteins have important roles in the adjustment of various cell functions and it has also been reported that similarities exist in the structures of catalytic domains of the participating protein kinases (Steven K. Hanks et al., Science, 1998, Vol. 241, pp. 42-52).
In recent years, the cloning of cDNAs of novel protein kinases by methods utilizing the above-noted structural similarties of protein kinases has been described in many reports (see, for example, Holtzman, D. et al., Proc. Natl. Acad. Sci. USA, 1987, 84, 8325-8329; Hanks, S. K., Proc. Natl. Acad. Sci. USA, 1987, 84 388-393; and Andrew F. Wilks, Proc. Natl. Acad. Sci. USA, 1989, vol. 86, pp. 1603-1607). With the advances in the studies in the field of interest, the analysis of the functions of novel protein kinase genes is in progress and the mechanisms of some important intracellular signal transduction are being elucidated but it can hardly be said that all mechanisms have been completely unravelled.
DISCLOSURE OF INVENTION
As described above, protein kinases obviously have diverse roles to play within cells. Therefore, isolating and identifying a novel protein kinase gene are expect
REFERENCES:
W.J. Fantl et al., "Signalling by Receptor Tyrosine Kinases", Annu. Rev. Biochem., vol. 62, pp. 453-481, 1993.
J.B. Bolen, "Nonreceptor Tyrosine Protein Kinases", Oncogene, vol. 8, pp. 2025-2031, Mar. 31, 1993.
R.J. Davis, "The Mitogen-Activated Protein Kinase Signal Transduction Pathway", The Journal of Biological Chemistry, vol. 268, No. 20, pp. 14553-14556, Jul. 15, 1993.
P. Nurse, "Universal Control Mechanism Regulating Onset of M-Phase", Nature, vol. 344, pp. 503-508, Apr. 5, 1990.
J. Pines, "Arresting Developments In Cell-Cycle Control", Trends. Biochem. Sci., vol. 19, pp. 143-145, Apr. 19, 1994.
D. Carling et al., "Mammalian AMP-Activated Protein Kinase Is Homologous to Yeast and Plant Protein Kinases Involved in the Regulation of Carbon Metabolism", The Journal of Biological Chemistry, vol. 269, No. 15, pp. 11442-11448, Apr. 15, 1994.
S.K. Hanks et al., "The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains", Science, vol. 241, pp. 42-52, Jul. 1, 1988.
S.K. Hanks, "Homology Probing: Identification of cDNA Clones encoding Members of the Protein-Serine Kinase Family", Proc. Natll. Acad. Sci. USA, vol. 84, pp. 388-392, Jan., 1987.
L. Tamagnone et al., "BMX, a Novel Nonreceptor Tyrosine Kinase Gene of the BTK/ITK/TEC/TXK Family Located In Chromosome Xp22.2", Oncogene, vol. 9, pp. 3683-3688, 1994.
M.R. Mark et al., "rse, a Novel Receptor-Type Tyrosine Kinase With Homology to Axl/Ufo, Is Expressed at High Levels in the Brain", The Journal of Biological Chemistry, vol. 269, No. 14, pp. 10720-10728, Apr. 8, 1994.
K. Ohashi et al., "Cloning of the cDNA for a Novel Receptor Tyrosine Kinase, Sky, Predominantly Expressed In Brain", Oncogene, vol. 9, pp. 699-705, 1994.
T. Karn et al., "Structure, Expression and Chromosomal Mapping of TKT From Man and Mouse: a New Subclass of Receptor Tyrosine Kinases With a Factor VIII-Like Domain", Oncogene, vol. 8, No. 12, pp. 3433-3440, 1993.
Chugai Seiyaku Kabushiki Kaisha
Elliott George C.
Schwartzman Robert
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