Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Transferase other than ribonuclease
Reexamination Certificate
1998-11-05
2001-01-09
Nashed, Nashaat (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Transferase other than ribonuclease
C435S252330, C435S254110, C435S320100, C536S023100, C536S023200, C536S023500
Reexamination Certificate
active
06171841
ABSTRACT:
BACKGROUND OF THE INVENTION
1. Field of the Invention
The present invention relates to a serine/threonine kinase, a DNA coding for said kinase, a recombinant vector comprising said DNA, a transformant transformed with said vector, and a process for preparing the serine/threonine kinase.
2. Prior Art
Various signals from the exterior of a cell are transmitted through receptors on the cell surface into the cell and ultimately into the necleus. The signals transmitted into the nucleus activate transcription factors and, as a result, expression of a group of genes is induced or repressed to produce phenotypes such as cell proliferation, differentiation and cell death. Many transcription factors have been cloned and the structure of functional domains have been elucidated: MOLECULAR BIOLOGY OF THE CELL THIRD EDITION, pp. 401-469. These functional domains are known to include leucine zipper, helix-loop-helix and zinc finger structures. Among them, the leucine zipper structure is a motif commonly found in such transcription factors as Jun/Fos, ATF/CREB and C/EBP families and these transcription factors form homo- or hetero-dimers through their leucine zipper structures to control the transcription of specific genes: Hai, T. et al., Proc. Natl. Acad. Sci., USA, 88:3720-3724 (1991).
Recently, it is reported that the leucine zipper structure is also found other functional molecules than the transcription factors (Holzman, L. B. et al., J. Biol. Chem., 269:30808-30817, 1994), suggesting that the leucine zipper structure not only facilitates the binding between transcription factors but also acts generally as a protein-protein interactional domain in cells.
Therefore, identification of molecules interacting with the leucine zipper domain is considered to be useful in analyzing not only new functions of transcription factors but also functions of the leucine zipper structure in other molecules than the transcription factors.
SUMMARY OF THE INVENTION
It is an object of the present invention to provide a serine/threonine kinase, a DNA coding for said kinase, a recombinant vector comprising said DNA, a transformant transformed with said vector, and a process for preparing the serine/threonine kinase.
As a result of their eager studies based on the above described problems, the present inventors have succeeded in isolating a DNA coding for a serine/threonine kinase from cDNA libraries prepared from human placenta and mouse brain and thus completed the present invention.
Accordingly, the present invention is the following recombinant protein (a) or (b):
(a) a protein comprising the amino acid sequence as shown in SEQ ID NO: 1;
(b) a protein comprising an amino acid sequence having one or several amino acids deleted, substituted or added in the amino acid sequence as shown in SEQ ID NO: 1, and exhibiting a serine/threonine kinase activity.
Also, the present invention is the following recombinant protein (c) or (d):
(c) a protein comprising the amino acid sequence as shown in SEQ ID NO: 2;
(d) a protein comprising an amino acid sequence having one or several amino acids deleted, substituted or added in the amino acid sequence as shown in SEQ ID NO: 2, and exhibiting a serine/threonine kinase activity.
Further, the present invention is a DNA coding for said protein. The DNA include, for example, those comprising the base sequence as shown in SEQ ID NO: 3 or 4.
The present invention is also a recombinant vector comprising said DNA.
Still further, the present invention is a transformant transformed with the recombinant vector.
Finally, the present invention is a process for producing a serine/threonine kinase comprising cultivating the transformant in a culture medium and collecting the serine/threonine kinase from the resulting culture.
REFERENCES:
Chien et al.; “The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest”; Proceedings of the National Academy of Sciences of USA; vol. 88; Nov. 1, 1991; pp. 9578-9582; XP000647704.
Holzman et al.; “Identification, .molecular cloning, and characterization of dual leucine zipper bearing kinase”; vol. 269, No. 49; 1994; pp. 30808-30817; XP002120730.
Kawai et al.; “ZIP kinase, a novel serine/threonine kinase which mediates apoptosis”; Molecular and Cellular Biology; vol. 18, No. 3; Mar. 1998; pp. 1642-1651; XP002120731.
Hillier et al.; “Homo sapienscDNA clone similar to DAP kinase”; EMBL Database Entry HS936258; Accession No. N23936; Dec. 30, 1995; Abstract; XP002120726.
Strausberg; “Homo sapienscDNA clone similar to DAP kinase”; EMBL Database Entry AA557328; Accession No. AA557328; Sep. 11, 1997; Abstract; XP002120727.
Marra et al.; “Mus musculus cDNA clone similar to DAP kinase”; EMBL Database Entry MMAA13041; Accession No. AA22667; Feb. 3, 1997; Abstract; XP002120729.
Akira Shizuo
Kawai Taro
Foley & Lardner
Japan Science and Technology Corporation
Nashed Nashaat
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