Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives
Reexamination Certificate
2005-12-22
2009-11-03
Desai, Anand U (Department: 1656)
Organic compounds -- part of the class 532-570 series
Organic compounds
Carbohydrates or derivatives
C435S252100, C424S450000
Reexamination Certificate
active
07612186
ABSTRACT:
A class of integral membrane proteins, referred to as Mistic polypeptides, their variants, fusion proteins including a Mistic polypeptide domain, and nucleic acid molecules encoding Mistic polypeptides and Mistic fusion proteins are disclosed herein. Also described are methods of using Mistic polypeptides and Mistic fusion proteins to produce and/or isolate recombinant proteins (including without limitation classes of eukaryotic proteins that have previously been intractable to recombinant bacterial expression, such as, eukaryotic integral membrane proteins).
REFERENCES:
patent: 5143846 (1992-09-01), Huala et al.
patent: 5264365 (1993-11-01), Georgiou et al.
patent: 5264366 (1993-11-01), Ferrari et al.
patent: 5508192 (1996-04-01), Georgiou et al.
patent: 5587455 (1996-12-01), Berger et al.
patent: 5668255 (1997-09-01), Murphy
patent: 5696237 (1997-12-01), FitzGerald et al.
patent: 5821082 (1998-10-01), Chinnadurai
patent: 5834209 (1998-11-01), Korsmeyer
patent: 5888732 (1999-03-01), Hartley et al.
patent: 6143557 (2000-11-01), Hartley et al.
patent: 6171861 (2001-01-01), Hartley et al.
patent: 6270969 (2001-08-01), Hartley et al.
patent: 6277608 (2001-08-01), Hartley et al.
patent: 6720140 (2004-04-01), Hartley et al.
patent: WO88/05821 (1988-08-01), None
patent: WO98/12328 (1998-03-01), None
patent: WO98/17682 (1998-04-01), None
patent: WO2004/015111 (2004-02-01), None
Baneyx and Georgiou, “In vivo degradation of secreted fusion proteins by theEscherichia coliouter membrane protease OmpT,”J. Bacteriol., 172:491-494, 1990.
Battiste and Wagner, “Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data,”Biochemistry, 39:5355-5365, 2000.
Berman et al., “The Protein Data Bank,”Nucleic Acids Research, 28:235-242, 2000.
Chaudhury and Smith, “Escherichia colirecBC deletion mutants,”J. Bacteriol., 160:788-791, 1984.
Derst and Karschin, “Evolutionary link between prokaryotic and eukaryotic K+ channels,”J. Exp. Biol., 201:2791-2799, 1998.
Elish, et al., “Biochemical analysis of spontaneous fepA mutants ofEscherichia coli,” J. Gen. Microbiol., 134:1355-1364, 1988.
Grzesiek and Bax, “A three-dimensional NMR experiment with improved sensitivity for carbonyl-carbonyl J correlation in proteins,”J. Biomol. NMR, 9:207-211, 1997.
Güntert et al., “Sequence-specific NMR assignment of proteins by global fragment mapping with the program MAPPER,”J. Biomol. NMR, 18:129-137, 2000.
Güntert, “Automated NMR structure calculation with CYANA,”Methods Mol. Biol., 278:353-378, 2004.
Hanahan et al. “Plasmid transformation ofEscherichia coliand other bacteria,”Meth. Enzymol., 204:63-113, 1991.
Hanes and Plückthun, “In vitro selection and evolution of functional proteins by using ribosome display”Proc. Natl. Acad. Sci. USA, 94:4937-4942, 1997.
Hilty et al., “Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents,”Chembiochem, 5:467-473, 2004.
Kiefer et al., “Bacterial expression of G-protein-coupled receptors: prediction of expression levels from sequence,”Receptors&Channels, 7:109-119, 2000.
Kobertz et al., “Hanging gondola structure of the T1 domain in a voltage-gated K+channel,”Biochem., 39:10347-10352, 2000.
Kosen, “Spin labeling of proteins,”Methods Enzymol., 177:86-121, 1989.
Laage et al., “Strategies for prokaryotic expression of eukaryotic membrane proteins,”Traffic, 2(2):99-104, 2001.
Lawler et al., “A rapid and efficient method for the radiosynthesis and purification of [125I]SCH23982,”J. Neurosci. Meth., 49:141-53, 1993.
McIntosh, et al., “Genetic and physiological studies on the relationship between colicin B resistance and ferrienterochelin uptake inEscherichia coliK-12,”J. Bacteriol., 137:653-657, 1979.
Needleman and Wunsch, “A general method applicable to the search for similarities in the amino acid sequence of two proteins,”J. Mol. Biol. 48:443-453, 1970.
Noren et al., “A general method for site-specific incorporation of unnatural amino acids into proteins,”Science, 244:182-188, 1989.
Oudega et al., “Analysis of theBacillus subtilisgenome: cloning and nucleotide sequence of a 62 kb region between 275° (rrnB) and 284° (pai)”,Microbiology, 143:2769-2774, 1997.
Pervushin et al., “Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution,”Proc. Natl. Acad. Sci. USA., 94:12366-12371, 1997.
Ramamurthy and Oliver, “Topology of the integral membrane form ofEscherichia coliSecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding ,”J. Biol. Chem., 272:23239-23246, 1997.
Riek et al., “Solution NMR techniques for large molecular and supramolecular structures,”J. Am. Chem. Soc., 124:12144-12153, 2002.
Ritter et al., “3D TROSY-HNCA(coded)CB and TROSY-HNCA(coded)CO experiments:triple resonance NMR experiments with two sequential connectivity pathways and high sensitivity,”J. Biomol. NMR, 28:289-294, 2004.
Roosild, et al., “NMR structure of Mistic, a membrane-integrating protein for membrane protein expression,”Science, 307:1317-1321, 2005.
Salzmann et al., “Improved sensitivity and coherence selection for [15N,1H]-TROSY elements in triple resonance experiments,”J. Biomol. NMR, 15:181-184, 1999.
Schatz and Dobberstein, “Common principles of protein translocation across membranes,”Science, 271:1519-1526, 1996.
Tate, “Overexpression of mammalian integral membrane proteins for structural studies,”FEBS Letters, 504:94-98, 2001.
Tucker et al., “Purification of a rat neurotensin receptor expressed inEscherichia coli,” Biochem. J., 317:891-899, 1996.
Veith etal., “The complete genome sequence of bacillus licheniformis DSM13, an organism with great industrial potential,”J. Mol. Microbiol. Biotechnol., 7:204-211, 2004.
Wimley and White, “Designing transmembrane alpha-helices that insert spontaneously,”Biochem., 39:4432-4442, 2000.
Choe Senyon
Greenwald Jason
Riek Roland
Roosild Tarmo
Desai Anand U
Klarquist & Sparkman, LLP
The Salk Institute for Biological Studies
LandOfFree
Compositions and methods for producing recombinant proteins does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Compositions and methods for producing recombinant proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Compositions and methods for producing recombinant proteins will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-4137599