Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving nucleic acid
Reexamination Certificate
2007-12-18
2007-12-18
Kim, Young J. (Department: 1637)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving nucleic acid
C435S091100, C435S091200
Reexamination Certificate
active
10689495
ABSTRACT:
A method and kit for synthesizing a nucleic acid molecule comprising at least one non-canonical nucleoside triphosphate using a double-mutant polymerase having a reduced discrimination between canonical and non-canonical substrates is disclosed. The method comprises incubating a template nucleic acid in a reaction mixture comprising the mutant nucleic acid polymerase and the appropriate canonical and non-canonical nucleoside triphosphates which are desired substrates for the mutant nucleic acid polymerase. The present invention is also a method of determining the sequence of a nucleic acid molecule using the mutant polymerase to create a nucleic acid molecule comprising at least one non-canonical nucleoside triphosphate.
REFERENCES:
patent: 4683195 (1987-07-01), Mullis et al.
patent: 0 655 506 (1995-05-01), None
Padilla et al., “A Y639/H784 T7 RNA polymerase double mutant displays superior properties for synthesizing RNAs with non-canonical NTPs,” Nucleic Acids Research, Dec. 2002, vol. 30, No. 24, e138, pp. 1-4.
“Probe Amplifier System Based on Chimeric Cycling Oligonucleotides,” Biotechniques 9(2):142-146, 1990.
W.M. Barnes, et al., “DNA Sequencing by Partial Ribosubstitution,” J. Mol. Biol. 119:83-99, 1978.
E.T. Butler and M.J. Chamberlin, “Bacteriophage SP6-specific RNA Polymerase,” J. Biol. Chem. 257(10):5772-5778, 1982.
C. Cazenave, et al., “RNA Template-directed RNA Synthesis by T7 RNA Polymerase,” PNAS 91:6972-6976, 1994.
D.H. Jones and B.H. Howard, “A Rapid Method for Recombination and Site-specific Mutagenesis by Placing Homologous Ends on DNA Using Polymerase Chain Reaction,”Biotechniques10(1):52-66, 1991.
G.A. Kassavetis, et al., “Bacteriophage SP6-specific RNA Polymerase,” J. Biol. Chem. 257(10):5779-5788, 1982.
D.A. Kostyuk, et al., “Mutants of T7 RNA Polymerase that are Able to Synthesize Both RNA and DNA,” FEBS Letters 369:165-168, 1995.
H. Kotani, et al., “Nucleotide Sequence and Expression of the Cloned Gene of Bacteriophage SP6 RNA Polymerase,” Nucl. Acids Res. 15(6):2653-2664, 1987.
R. Sousa and R. Padilla, “A Mutant T7 RNA Polymerase as a DNA Polymerase,” EMBO J. 14(18):4609-4621, 1995.
E. Uhlman, et al., “Antisense Oligonucleotides: A New Therapeutic Principle,” Chem. Rev. 90:543-593, 1990.
A. Wolfgang, et al., “Kinetic Characterization of Ribonuclease-resistant 2′-modified Hammerhead Ribozymes,” Science 253:314-317, 1991.
Bonner, et al., “Mutations in T7 RNA polymerase that support the proposal for a common poymerase active site structure,” The EMBO Journal 11:3767-3775 (1992).
Bonner et al., “Characterization of a Set of T7 RNA Polymerase Active Site Mutants,” The Journal of Biological Chemistry 269:25120-25128 (1994).
Brieba, et al., “Role of T7 Polymerase His784 in Start Site Selection and Initial Transcription,” Biochemistry 41:5144-5149 (2002).
Cheetham et al., “Structure of a Transcribing T7 RNA Polymerase Initiation Complex,” Science 286:2305-2309 (1999).
Cunningham et al, “Use of Inorganic Pyrophosphatase to Improve the Yield of In Vitro Transcription Reactions Catalyzed by T7 RNA Polymerase,” BioTechniques 9:713-714 (1990).
Delarue, et al., “An attempt to unify the structure of polymerases,” Protein Engineering 3:461-467 (1990).
Huang et al., “Mechanism of Ribose 2′-Group Discrimination by an RNA Polymerase,” Biochemistry 36:8231-8242 (1997).
Huang et al., “Misincorporation by Wild-Type and Mutant T7 RNA Polymerases: Identification of Interactions that Reduce Misincorporation Rates by Stabilizing the Catalytically Incompetent Open Conformation” Biochemistry 39:11571-11580 (2000).
Makarova et al., “Transcribing ofEscherichia coligenes with mutant T7 RNA polymerases: Stability of lacZ mRNA inversely correlates with polymerase speed,” Proc. Natl. Acad. Sci. USA 92:12250-12254 (1995).
Mentesana et al., “Characterization of Halted T7 RNA Polymeraase Elongation Complexes Reveals Multiple Factors that Contribute to Stability,” J. Mol. Biol. 302:1049-1062 (2000).
Moroney et al., “Abortive Products as Initiating Nucleotides during Transcription by T7 RNA Polymerase,” Biochemistry 30:10343-10349 (1991).
Osumi-Davis et al., “Bacteriophage T7 RNA Polymerase and Its Active-site Mutants,” J. Mol. Biol. 237:5-19 (1994).
Padilla et al., “Efficient Synthesis of nucleic acids heavily modified with non-canonical ribose 2′-groups using a mutant T7 RNA polymerase (RNAP),” Nucleic Acids Research 27:1561-1563 (1999).
Padilla et al., “A Y639F/H784A T7 RNA polymerase double mutant displays superior properties for synthesizing RNAs with non-canonical NTPs,” Nucleic Acids Research 30:e138 (2002).
Patra et al., “Isolation and Characterization of Mutant Bacteriophage T7 RNA Polymerases,” J. Mol. Biol. 224:307-318 (1992).
Tabor et al., “A Bacteriophage T7 RNA Polymerase/Promoter System for Controlled Exclusive Expression of Specific Genes,” Proc. Natl. Acad. Sci. USA 82:1074-1078 (1985).
Tabor et al., “Effect of manganese ions on the incorporation of dideoxynucleotides by bacteriophage T7 DNA polymerase andEscherichia coliDNA polymerase I,” Proc. Natl. Acad. Sci. USA 86:4076-4080 (1989).
Zhang et al., “Protein quantification from complex protein mixtures usign a proteomics methodology with single-cell resolution,” PNAS 98:5497-5502 (2001).
Kim Young J.
Quarles & Brady LLP
University of Texas
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