Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Reexamination Certificate
2006-04-18
2006-04-18
Ketter, James (Department: 1633)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
C435S320100, C435S069600
Reexamination Certificate
active
07029876
ABSTRACT:
Vectors for producing polypeptides heterologous to prokaryotes are described comprising, along with the polypeptide-encoding nucleic acid, anti-termination nucleic acid that inhibits intragenic transcription termination with a non-lambda promoter therefor and/or nucleic acid encoding a GreA or GreB protein and a promoter therefor. Also described are processes for producing a heterologous polypeptide in prokaryotic host cells utilizing such elements to improve the quality and/or quantity of heterologous polypeptide produced.
REFERENCES:
patent: 4578355 (1986-03-01), Rosenberg
patent: 5162217 (1992-11-01), Hartman et al.
patent: 5256546 (1993-10-01), Aviv et al.
patent: 5354846 (1994-10-01), Kehoe
patent: 5374520 (1994-12-01), Milman
patent: 5401658 (1995-03-01), Fiers et al.
patent: 5618715 (1997-04-01), Shoyab et al.
patent: 5834184 (1998-11-01), Harada et al.
patent: 131843 (1985-01-01), None
patent: 314184 (1989-05-01), None
patent: 457676 (1992-01-01), None
patent: 691406 (1996-01-01), None
patent: 700997 (1996-03-01), None
patent: 838525 (1998-04-01), None
patent: 893502 (1999-01-01), None
patent: 9059299 (1997-03-01), None
patent: WO 85/02624 (1985-06-01), None
patent: WO 85/04418 (1985-10-01), None
patent: WO 88/06628 (1988-09-01), None
patent: WO 89/03886 (1989-05-01), None
Hasan N, Szybalski W, Control of cloned gene expression by promoter iversion in vivo: cibstruction of improved vectors with a multiple cloning site and the ptac promoter, 1987, Gene, 56:145-151.
Li S, Li F, Wu W, Tan W, Yu M, Chen J, Tao K, Expression inEscherichia coliand purification of human thrombopoietin, 1997, Biotechnol. Appl. Biochem. 26: 15-17.
Clements DA, Wang JK, Dionne CA, Goldfarb M, Activation of fibroblast growth factor (FGF) receptors by recombinant human FGF-5, 1993, Oncogene, 8:1311-1316.
Loizos and Darst., “Mapping Interactions ofEscherichia coliGreB with RNA Polymerase and Ternary Elogation Complexes.”J. Bio. Chem. 274(33) :23378-23386 (Aug. 1999).
Seltas et al., “Expression Plasmid with a Very Tight Two-Step Control: Int/att-Mediated Gene Inversion with Respect to the Stationary Promoter.”Gene. 267:213-220 (Apr. 2001).
Shatzman and Rosenberg., “the pAS Vector System and Its Application to Heterologous Gene Expression inEscherichia coli.”Hepatology. (Suppl. 1) 7(1):305-355 (Jan. 1987).
Beck et al., “Efficient Production of Active Human Manganese Superoxide Dismutase inEscherichia coli.” Biotechnology, 6:930-935 (Aug. 1988).
Bielawski et al., “Construction of a DNA-Polymerase I Overproducing Plasmid and Isolation of the Enzyme.”Acta Biochim. Pol. 34(1):29-34 (1987).
Borukhov and Goldfarb., “Purification and Assay ofEscherichia coliTranscript Cleavage Factors GreA and GreB.”Meth. Enzymol., 274:315-326 (1996).
Borukhov et al., “GreA Protein: A Transcription Elongation Factor FromEscherichia coli.” Proc. Natl. Acad. Sci. USA89:8899-8902 (Oct. 1992).
Borukhov et al., “Transcript Cleavage Factors fromE. coli.” Cell. 72:459-466 (Feb. 1993).
Chauhan and Apirion., “The Gene for a Small Stable RNA (10Sa RNA) ofEscherichia coli.” Molecular Microbiology. 3(11):1481-1485 (1989).
Darst et al., “Crystallization of GreA, A Transcript Cleavage Factor FromEscherichia coli.” J. Mol. Bio. 242:582-585 (1994).
Das., “Transcription Antitermination by Lambda N Gene Product in a Well Defined Plasmid System.”Fed. Proc. (72nd Anual Mtg. Amer. Soc. Bio. Chem.—Abstract 1291) 40(6):1764 (May 31-Jun. 4, 1981).
Erie et al., “Multiple RNA Polymerase Conformations and GreA: Control of the Fidelity of Transcription.”Science. 262:867-873 (1993).
Feng et al., “GreA- Induced Transcript Cleavage in Transcription Complexes ContainingEscherichia coliRNA Polymerase Is controlled by Multiple Factors, Including Nascent Transcript Location and Structure.”J. Bio. Chem. 269:22282-22294 (1994).
Feng et al., “Interactions Between RNA Polymerase and Transcript Affect GreA- And Gre-B-Mediated Reverse Translocation.”J. Cell. Biochem. Suppl. (Abstract L408) 18C:58 (1994).
Franklin and Bennett., “The “N” Protein of Bacteriophage Lambda, Defined by its DNA Sequence, Is Highly Basic.”Gene. 8:107-119 (1979).
Franklin., “N Transcription Antitermination Proteins of Bacteriophages λ. φ21 and F22”.J. Mol. Bio. 181:85-91 (1985).
Franklin., “Clustered Arginine Residues of Bacterlophage λ N Protein are Essential to Antitermination of Transcription, but Their Locale Cannot Compensate for boxB Loop Defects.”J. Mol. Bio. 231:343-360 (1993).
Franklin., “conservation of Genome Form but not Sequence in the Transcription Antitermination Determinants of Bacteriophages λ, φand P22.”J. Mol. Bio. 181:75-88 (1984).
Friedman and Olson., “Evidence that a Nucleotide Sequence, “boxA,” Is Involved in the Action of the NusA Protein.”Cell. 34:143-149 (1983).
Friedman et al., “Transcription-Dependent Competition for a Host Factor: The Function and Optimal Sequence of the Phage λboxA Transcription Antitermination Signal,”Genes Dev. 4:2210-2222 (1990).
Garcia et al., “TheE. colidnaY Gene Encodes an Arginine Transfer RNA.”Cell. 45:453-459 (1986).
Gatenby and Castleton., “Amplification of Miaze Ribulose Bisphosphate Carboxylase Large Subunit Synthesis inE. coliby Transcriptional Fusion with the Lambda N Operon.”Mol. Gen. Genet. 185:424-429 (1982).
Greenblatt et al., “Transcriptional Antitermination.”Nature. 364:401-406 (Jul. 1993).
Gu et al., “Nascent RNA Cleavage by Arrested RNA Polymerase II Does Not Require Upstream Translocation of the Elongation Complex on DNA.”J. Bio. Chem. 268:25604-25616 (1993).
Guo and Price., “Mechanism of DmS-II-Mediated Pause Suppression by Drosophila RNA Polymerase II.”J. Bio. Chem. 268:18762-18770 (1993).
Horiuchi et al., “Effects of pH on Expression and Stabilization of β-Galactosidase by RecombinantE. coliwith a Thermally-Induced Expression System.”Biotechnology Lett. 16:113-118 (1994).
Hsu et al., “Escherichia coliTranscript Cleavage Factors GreA and GreB Stimulate Promoter Escape and Gene Expression In Vivo and In Vitro.”Proc. Natl. Acad. Sci. USA92:11588-11592 (1995).
Hwang et al., “High Level Expression of Porcine Growth Hormone inEscherichia coliFrom an Expression Vector Containing Bacteriophage λ PL and N Gene Untrasnlated Region.”Biochem.&Biophys. Res. Comm. 173:711-717 (1990).
Izban and Luse., “Factor-Stimulated RNA Polymerase II Transcribes at Physiological Elongation Rates on Naked DNA but Very Poorly on Chromatin Templates.”J. Bio. Chem. 267(19):13647-13655 (1992).
Izban and Luse., “SII-Facilitated Transcript Cleavage in RNA Polymerase II Complexes Stalled Early After Initiation Occurs in Primarily Dinucleotide Increments.”J. Bio. Chem. 268(17):12864-12873 (1993).
Izban and Luse., “The Increment of SIM-Facilitated Transcript Cleavage Varies Dramatically Between Elongation Competent and Incompetent RNA Polymerase II Ternary Complexes.”J. Bio. Chem. 268(17):12874-12885 (Jun. 1993).
Izban and Luse., “The RNA Polymerase II Ternary Complex Cleaves the Nascent Transcript in a 3′→ 5′Direction in the Presence of Elongation Factor SII.”Genes&Development6:1342-1356 (1992).
Kanasawa et al., “Optimization of β-Galactosidase Production by RecombinantE. coliwith Thermo-Inducible Expression System.”IFAC Symp. Ser. 10:255-258 (1992).
Kassavetis and Geiduschek., “RNA Polymerase Marching Backward.”Science. 259:944-945 (Feb. 1993).
Keiler et al., “Role of a Peptide Tagging System in Degradation of Proteins Synthesized from Damaged Messenger RNA.”Science. 271:990-993 (Feb. 1996).
Koulich et al., “Distinct Function on N and C-Terminal D
Paegle Eriks Sasha
Reilly Dorothea
Yansura Daniel G.
Genentech Inc.
Hasak Janet E.
Ketter James
Riggins Patrick S.
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