Chemistry: molecular biology and microbiology – Vector – per se
Reexamination Certificate
2011-03-22
2011-03-22
Desai, Anand U (Department: 1656)
Chemistry: molecular biology and microbiology
Vector, per se
C435S069100, C435S252100, C435S325000, C536S023100, C536S023400
Reexamination Certificate
active
07910364
ABSTRACT:
A recombinant expression system for the expression of a poly amino acid, peptide or protein is provided. The poly amino acid of interest is expressed as a fusion protein that includes an amino acid sequence recognized and cleaved by a Ulp1 protease. The amino acid sequence joined to the poly amino acid of interest is preferably from a SUMO (small ubiquitin-like molecule) protein. This sequence imparts favorable solubility and refolding properties to the fusion protein. A purification tag may also be incorporated into the fusion protein for ease of isolation. This recombinant expression system is particularly advantageous for expression and rapid and highly specific cleavage and purification of poly amino acids that have low solubilities or are difficult to express in other systems.
REFERENCES:
patent: 5643758 (1997-07-01), Guan et al.
patent: 6872551 (2005-03-01), Lima et al.
patent: 7060461 (2006-06-01), Butt et al.
patent: 7498165 (2009-03-01), Lima et al.
Yoshinobu Ichimura, Takayoshi Kirisako, Toshifumi Takao, Yoshinori Satomi, Yasutsugu Shimonishi, Naotada Ishihara, Noboru Mizushima, Isei Tanida, Eiki Kominami, Mariko Ohsumi, Takeshi Noda and Yoshinori Ohsumi, “A ubiquitin-like system mediates protein lipidation”, Nature (2000) 408: 488-492.
Elena Mossessova and Christopher D. Lima, “Ulp1-SUMO Crystal Structure and Genetic Analysis Reveal Conserved Interactions and a Regulatory Element Essential for Cell Growth in Yeast”, Molecular Cell (2000) 5: 865-876.
Edward T.H. Yeh, Limin Gong, Tetsu Kamitani, “Ubiquitin-like proteins: new wines in new bottles”, Gene (2000) 248: 1-14.
Shyr-Jiann Li and Mark Hochstrasser, “The Yeast ULP2 (SMT4) Gene Encodes a Novel Protease Specific for the Ubiquitin-Like Smt3 Protein”, Molecular and Cellular Biology (2000) 20: 2367-2377.
Katsunori Tanaka, Junko Nishide, Koei Okazaki, Hiroaki Kato, Osami Niwa, Tsuyoshi Nakagawa, Hideyuki Matsuda, Makoto Kawamukai, and Yota Murakami, “Characterization of a Fission Yeast SUMO-1 Homologue, Pmt3p, Required for Multiple Nuclear Events, Including the Control of Telomere Length and Chromosome Segregation”, Molecular and Cellular Biology (1999) 19: 8660-8672.
Shyr-Jiann Li and Mark Hochstrasser, “A new protease required for cell-cycle progression in yeast”, Nature (1999) 398: 246-251.
David P. Lane and Peter A. Hall, “SUMO-1: wrestling with a new ubiquitin-related modifier”, TIBS (1997) 22:374-376.
Erica S. Johnson, Ingrid Schwienhorst, R. Jürgen Dohmen, and Günter Blobel, “The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer”, The EMBO Journal (1997) 16: 5509-5519.
Kohno et al., “A new general method for the biosynthesis of stable isotope-enriched peptides using a decahistidine-tagged ubiquitin fusion system: An application to the production of mastoparan-X uniformly enriched with 15N and 15N/13C”, (Journal of Biomolecular NMR, 1998, 12:109-121).
Wang et al., “Biotin-Ubiquitin Tagging of Mammalian Proteins inEscherichia coli”, Protein Expression and Purification, 30:140-149 (2003).
Yaseen et al., “Two Distinct Classes of Ran-Binding Sites on the Nucleoporin Nup-358”, Proc. Natl. Acad. Sci, vol. 96, p. 5516-5521 (1999).
Stanton et al., “Analysis of the Human Herpervirus-6 Immediate-Early 1 Protein”, Journal of General Virology, 83, p. 2811-2820 (2002).
Muller et al., “Conjugation with the Ubiquitin-Related Modifier SUMO-1 Regulates the Partitioning of PML Within the Nucleus”, The EMBO Journal, vol. 17, No. 1, p. 61-70 (1998).
Poukka, et al., “Ubc9 Interacts with the Androgen Receptor and Activates Receptor-Dependent Transcription”, Journal of Biological Chemistry, vol. 274, No. 27, p. 19441-19446 (1999).
Champion pET SUMO Protein Expression System (Invitrogen Instruction Manual) Version A Jan. 27, 2004.
Melchior, F., “SUMO-Nonclassical Ubiquitin”, Annu. Rev. Cell Dev. Biol., 16:591-626 (2000).
Chosed et al., “Evolution of a Signalling System that Incorporates both Redundancy and Diversity:ArabidopsisSUMOylation”, Biochem J. 398, 521-529 (2006).
Hannig, et al., “Strategies for Optimizing Heterologous Protein Expression inEscherichia coli”, Trends in Biotechnol., 16:54-60 (1998).
Rosenfeld, S., “Use ofPichia pastorisfor Expression of Recombinant Proteins”, Methods in Enzymology, 306:154-169 (1999).
Product Catalog by LifeSensor, Inc. entitled “SUMOpro® -3 Expression Vector” (2006).
Cookson, “Pathways to Parkinsonism”, Neuron, vol. 37, 7-10 (2003).
Hockstrasser, “Evolution and Function of Ubiquitin-Like Protein-Conjugation Systems”, Nature Cell Biology, vol. 2 p. E153-E157(2000).
Johnson et al., “Cell Cycle-Regulated Attachment of the Ubiquitin-Related Protein SUMO to the Yeast Septins”, Journal of Cell Biology, vol. 147, No. 5, p. 981-993 (1999).
Li et al., “The Yeast ULP2 (SMT4) Gene Encodes a Novel Protese Specific for the Ubiquitin-Like Smt3 Protein”, Molecular and Cellular Biology, vol. 20, No. 7, p. 2367-2377 (2000).
Li et al., “The Ulp1 SUMO Isopeptidase: Distinct Domains Required for Viability, Nuclear Envelope Localization, and Substrate Specificity”, Journal of Cell Biology, vol. 160, No. 7, p. 1069-1-81 (2003).
Matunis, et al., “A Novel Ubiquitin-Like Modification Modulates the Partitioning of the Ran-GTPhase-Activating protein Ran GAP1 Between the Cytosol and the Nuclear Pore Complex”, Journal of Cell Biology, vol. 135, No. 6, Pt. 1, p. 1457-1470 (1996).
Guzzo et al., “Systematic Analysis of Fusion and Affinity Tags Using Human Aspartyl-tRNA Synthetase Expressed inE. coli”, Protein Expression and Purification 54, p. 166-175 (2007).
Rao-Naik et al., “The Rub Family of Ubiquitin-Like Proteins”, Journal of Biological Chemistry, vol. 273, No. 52, p. 34976-34982 (1998).
Reverter, et al., “A Basis for SUMO Protease Specificity Provided by Analysis of Human Senp2 and a Senp2-SUMO Complex”, Structure, vol. 12, p. 1519-1531 (2004).
Schwartz et al., “A Superfamily of Protein Tags: Ubiquitin, SUMO and Related Modifiers”, Trends in Biochemical Sciences, vol. 28, No. 6, p. 321-328 (2003).
Shi et al., “Association of FHIT (Fragile Histidine Triad), a Candidate Tumour Suppressor Gene, with the Ubiquitin-Conjugating Enzyme hUBC9”, Biochem J., 352, 443-448 (2000).
Weeks, et al., Ligation Independent Cloning Vectors for Expression of SUMO Fusions, Protein Expression and Purification 53, 40-50 (2007).
Lima Christopher D.
Mossessova Elena
Cornell Research Foundation Inc.
Desai Anand U
Hoffmann & Baron , LLP
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