Synthesis of peptides as cloned ubiquitin extensions

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...

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435 691, 4351723, 4352523, 4353201, 530412, 530324, 530350, C12N 1562

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057632251

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
patent: 5132213 (1992-07-01), Bachmair
patent: 5156968 (1992-10-01), Liu
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 Disorder, 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.
Jonnalagadds, 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 Carboyyl-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 corporaiton, 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 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 Characterizaiton of the Carboxyl-Terminal Ethyl Ester of Ubiquitin, Abstracts from the ASBC/DBC, ACS meeting, 14 Jan., 1986.
PTO Manual of Patent Classification, 530-1--530-3, Dec. 1990.
Butt et al., "Ubiquitin Fusion Augments the Yield of Cloned Gene Products in Escherichia coli," PNAS USA, 86:2540-2544 (1989).
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).
Creighton, T.E., ed Proteins, Structures and Molecular Properties, WH Freeman and Co., New York, 1993, pp.466-468.
Kane and Hartley, Formation of Recombinant Protein Inclusion Bodies in Escherichia coli, Trends, Biotechnol. 6:95-101 (1988).
Rechsteiner, et al., Protein Structure and Instracellular Stability, TIBS 12:390-394 (1987).
Butt, et al., Ubiquitin-Metallothionein Fusion Protein Expression in Yeart, J. Biol. Chem. 263:16364-16371 (1988).
Wilkinson, et al., Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases, Biochemical Sociey Transactions 20:631-637 (1992).
Mayer, Master's Thesis, Emory University, 1986.
Rose and warms, An Enzyme with UIbiuitin Carboxy-Terminal Esterase Activity from Reticulocytes, Biochemistry 22:4234-4257 (1983).
Ozkaynak et al., "The Yeast Ubiauitin Gene: A Family of Natural Gene Fusions," EMBO J, 6:1429-1439, May 1987.
Jonnalagadda et al., "Expression and Accurate Processing of Yeast Penta-ubiquitin in Escherihia coli," Journal of Biological Chemistry, 262(36):17750-17756, 1987.

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