Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Patent
1992-04-03
1997-04-15
Draper, Garnette D.
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
435 691, 4352523, 4353201, 530412, 536 234, C12N 1562
Patent
active
056209231
ABSTRACT:
A method for the preparation of synthetic peptide products containing up to about forty amino acid residues as ubiquitin-carboxyl terminal extensions expressed in procaryotic cells such as E. coli is disclosed. This is accomplished by cloning appropriate oligonucleotides encoding the desired peptide as a ubiquitin peptide extension gene, splicing the gene into an appropriate plasmid which, in turn is transformed into E. coli, or other appropriate procaryotic cells and inducing expression of the ubiquitin peptide fusion product. When expressed, the cells produce recoverable amounts of ubiquitin extended at its carboxyl terminus by the encoded carboxyl terminal extended peptide (CTEP). The peptide can be recovered as ubiquitin fused extension products (Ub-CTEP) or, alternatively, can be cleaved from the ubiquitin by an appropriate eucaryotic peptidase and purified. The process is adaptable to the production of any desirable peptide containing from 2 to about 40 amino acid residues and is particularly adaptable to the production of peptides containing between about 5 and 40 amino acid residues.
REFERENCES:
patent: 5093242 (1992-03-01), Bachmair et al.
patent: 5132213 (1992-07-01), Bachmair
patent: 5156968 (1992-10-01), Liu
EMBO, J. 6:1424-1439, May 1987, Ozkaghak et al. The Yeast Ubiquitin Gene: a Family of Natural Gene Fusions.
Yoo and Rechsteiner, Anal. Biochem., 191;35-40, 1990.
Wilkinson, Methods in Enzymology, 185:387-397, 1990.
Lowe, et al., Ubiquitin Carboxyl-Terminal Hydrolase (PGP 9.5) is Selectively Present in Ubiquitinated Inclusion Bodies Characteristic of Human Degenerative Diseases, J. Pathol. 161:153-160, 1990.
Mayer et al., Abstract from the Second International Conference on Alzheimer's Disease and Related Disorders, Toronto, Canada, 15-20 Jul., 1990.
Wilkinson, et al., Abstract from the ASBMB/AAI Meeting, 1990.
Liu et al., J. Biol. Chem. 264(34):20331-20338, 1989.
Wilkinson, et al., The Neuron-Specific Protein PGP 9.5 Is a Ubiquitin Carboxyl-Terminal Hydrolase, Science, 246:670-673, 1989.
Yoo, et al., J. Biol. Chem., 264(29):17078-17083, 1989.
Miller, et al., Bio/Technology, 7:698-704, 1989.
Jonnalagadda, J.Biol.Chem., 264(18):10637-10642, 1989.
Ecker, et al., J. Biol. Chem., 264(13):7715-7719, 1989.
Monia, J. Biol. Chem., 264(7):4093-4103, 1989.
Mayer & Wilkinson, Detection, Resolution, and Nomenclature of Multiple Ubiquitin Carboxyl-Terminal Esterases from Bovine Calf Thymus, Biochemistry, 28;166-172, 1989.
Duerksen-Hughes, Affinity Chromatography Using Protein Immobilized via Arginine Residues, Biochemistry, 28:8530-8536, 1989.
Wilkinson, Ubiquitin, Ed. M. Rechsteiner, Plenum Publishing Corporation, 1988, pp. 5-38.
Booth, et al., J. Biol. Chem., 263(31):16364-16371, 1988.
Ecker, et al., J. Biol. Chem., 262(29):14213-14221, 1987.
Ecker, et al., J. Biol. Chem., 262(8):3524-3527, 1987.
Wilkinson, Protein Ubiquitination: a regulatory post-translational modification, Anti-Cancer Drug Design, 2;211-229, 1987.
Duerksen-Hughes, Biochemistry, 26:6980-6987, 1987.
Bachmair, et al., In Vitro Half Life of a Protein is a Function of its Amino Terminal Residue, Science, 234:179-186, 1986.
Wilkinson, et al., Synthesis and Characterization of Ubiquitin Carboxyl-Terminal Hydrolase, Biochemistry, 25:6644-6649, 1986.
Wilkinson, et al., Synthesis and Characterization of the Carboxyl-Terminal Ethyl Ester of Ubiquitin, Abstracts from the ASBC/DBC, ACS meeting, 14 Jan., 1986.
Pickart and Rose, Ubiquitin Carboxyl-Terminal Hydrolase Acts on Ubiquitin Carboxyl-Terminal Amides, J. Biol. Chem. 260:7903-7910 (1985).
Cox, et al., Tryptic Peptide Mapping of Ubiquitin and Derivatives Using Reverse Phase HPLC, Analytical Biochemistry, 154: 345-352, (1986).
Kane and Hartley, Formation of Recombinant Protein Inclusion Bodies in Escherichia coli, Trends, Biotechnol. 6:95-101 (1988).
Bachmair, et al., US patent application No. 07/178,924, Filed Apr. 7, 1988, Amendment dated May, 1990, pp. 6-7, in Prosecution History.
Rechsteiner, et al., Protein Structure and Intracellular Stability, TIBS 12:390-394 (1987).
Wilkinson, et al., Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases, Biochemical Society Transactions 20:631-637 (1992).
Mayer, Master's Thesis, Emory University, 1986.
Rose and Warms, An Enzyme with Ubiquitin Carboxy-Terminal Esterase Activity from Reticulocytes, Biochemistry 22:4234-4237 (1983).
P.N.A.S. 86:2540-2544, Apr., 1989, Butt et al Ubiquitin Fusion Augments the Yield of Cloned Gene Products in Escherichia coli.
J. Biol. Chem. 263:16364-16371, Nov. 5, 1988, Butt et al. Ubiquitin-Metallothiorein Fusion Protein Expression in Yeast.
Rechsteiner Martin C.
Rote Kevin V.
Wilkinson Keith D.
Yoo Yung
Draper Garnette D.
The University of Utah
Ulm John R.
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