Method and system for rapid biomolecular recognition of...

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving antigen-antibody binding – specific binding protein...

Reexamination Certificate

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C435S287100, C435S287200, C436S501000, C436S503000, C436S063000, C436S086000, C436S172000

Reexamination Certificate

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06846638

ABSTRACT:
Methods, compositions, kits, and apparatus are provided wherein the aminoacyl-tRNA synthetase system is used to analyze amino acids. The method allows very small devices for quantitative or semi-quantitative analysis of the amino acids in samples or in sequential or complete proteolytic digestions. The methods can be readily applied to the detection and/or quantitation of one or more primary amino acids by using cognate aminoacyl-tRNA synthetase and cognate tRNA. The basis of the method is that each of the 20 synthetases and/or a tRNA specific for a different amino acid is separated spatially or differentially labeled. The reactions catalyzed by all 20 synthetases may be monitored simultaneously, or nearly simultaneously, or in parallel. Each separately positioned synthetase or tRNA will signal its cognate amino acid. The synthetase reactions can be monitored using continuous spectroscopic assays. Alternatively, since elongation factor Tu:GTP (EF-Tu:GTP) specifically binds all AA-tRNAs, the aminoacylation reactions catalyzed by the synthetases can be monitored using ligand assays. Microarrays and microsensors for amino acid analysis are provided. Additionally, amino acid analysis devices are integrated with protease digestions to produce miniaturized enzymatic sequenators capable of generating either N- or C-terminal sequence and composition data for a protein or peptide. The possibility of parallel processing of many samples in an automated manner is discussed.

REFERENCES:
patent: 5111221 (1992-05-01), Fare et al.
patent: 5183740 (1993-02-01), Ligler et al.
patent: 5225374 (1993-07-01), Fare et al.
patent: 5354654 (1994-10-01), Ligler et al.
patent: 5643722 (1997-07-01), Rothschild et al.
patent: H1775 (1999-01-01), Ligler et al.
patent: 6007690 (1999-12-01), Nelson et al.
patent: 6020209 (2000-02-01), Narang et al.
patent: 6100541 (2000-08-01), Nagle et al.
patent: 6103199 (2000-08-01), Bjornson et al.
patent: 6165335 (2000-12-01), Lennox et al.
patent: 6221640 (2001-04-01), Tao et al.
Berg. B. H., “Purification of Aminoacyl-tRNA Synthetase Kinase Activities Associated with Threonyl- and Tyrosyl-tRNA Synthetases Isolated from Bom:NMRI Mouse Liver”, Bioch. Mol. Biol. Int., vol. 29, pp. 949-958 (1993).*
Schmitt, A. P. et al., “Msn2p, a zinc finger DNA-binding protein, is the transcriptional activator of the multistress response inSaccharomyces cerevisiae”, PNAS, vol. 93, pp. 5777-5782 (1996).*
Beaulande, M. et al., “Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression inEscherichiaco and characterization as human autoantigen”, Nucl. Acids Res., vol. 26, pp. 521-524 (1998).*
Shipwash. “Microarrays for Amino Acid Analysis and Protein Sequencing” Aug. 10, 1999, NanoNano Technology, vol. 1, pp. 1-21.*
VWR International “Molecular size exclusion chromatography”, 2000, pp. 1-2.*
Demandolx, D “Guidelines for multifluorescence confocal imaging: acquisition, processing and display” 1997, Microscopy and Analysis, vol. 48, pp. 5-7.*
Schimmel, P., “Aminoacyl tRNA Synthetases: General Scheme of Structure-Function Relationships in the Polypeptides and Recognition of Transfer RNAs”,Annu. Rev. Biochem., 56:125-158 (1987).
Freist, W., “Mechanisms of Aminoacyl-tRNA Synthetases: A Critical Consideration of Recent Results”,Biochemistry, 28:6787-6795 (1989).
Schimmel, P., “Aminoacylaton of RNA oligonucleotides: minimalist structures and origin of specificity”,FASEB J., 7:282-9 (1993).
Cusack, S., “Aminoacyl-tRNA synthetases”,Curr. Opin. Struc. Biol., 7:881-9 (1997).
Negrutskii et al., “Functional Interaction of Mammalian Valyl-tRNA Synthetase with Elongation Factor EF-1α in the Complex with EF-1H”,JBC, 274:4545-4550 (1999).
Lloyd et al., “A broadly applicable continuous spectrophotometric assay for measuring aminoacyl-tRNA synthetase activity”,Nucl. Acids. Res., 23:2886-2892 (1995).
Reed et al., “Mechanisms of the Transfer of Aminoacyl-tRNA from Aminoacyl-tRNA Synthetase to the Elongation Factor 1α”,JBC, 269:32932-36 (1994).
Lechler et al., “Overproduction of Phenylalanyl-tRNA Synthetase fromThermus thermophilusHB8 inEscherichia coli”, Protein Expr. Purif., 8:347-57 (1996).
Bausch et al., “Analysis and overexpression inEscherichia coliof astaphylococcalgene encoding seryl-tRNA synthetase”,Biochim. Biophys. Acta, 1397:169-74 (1998).
Martinis et al., “Aminoacyl-tRNA synthetases: A new image for a classical family”,Biochimie, 81:683-700.
Schimmel et al., “Aminoacyl tRNA synthetases as targets for new anti-infectives”,FASEB J., 12:1599-609 (1998).
DeGuzman et al., “Protein—RNA Recognition”,Biopolymers(Nucleic Acid Sciences), 48:181-95 (1998).
Freist et al., “Glutamyl-tRNA Synthetase”,Biol. Chem., 378:1313-29 (1997).
Freist et al., “Glycyl-tRNA Synthetase”,Biol. Chem., 377:343-56 (1996).
Cusak, S., “Eleven down and nine to go”,Nat. Struct. Biol., 2:824-31 (1995).
Fukai, S., “Structural Basis for Double-Sieve Discrimination of L-Valine from L-Isoleucine and L-Threonine by the Complex of tRNAValand Valyl-tRNA Synthetase”,Cell, 103:793-803 (2000).
Ibba et al., “Aminoacyl-tRNA Synthesis”,Ann Rev. Biochem. Sci., 69:617-50 (2000).
Ibba et al., “The Adaptor hypothesis revisited”,Trends Biochem., 25:311-6.
Freist et al., “Histidyl-tRNA Synthetase”,Biol. Chem., 380:623-46 (1999).
Cavarelli et al., “Recognition of tRNAs by aminoacyl-tRNA synthetases”,FASEB J., 7:79-86 (1993).
Webb, M.R., “A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems”,Proc. Nat'l Acad. Sci. USA, 89:4884-4887 (1992).
Pellequer et al., “Measurement of kinetic binding constants of viral antibodies using a new biosensor technology”,J. Immunol. Meth., 166:133-143 (1993).
Blank et al., “Overexpression and Purification ofThermus thermophilusElongation Factors G, Tu, and Ts fromEscherichia coli”, Protein Expr. Purif., 6:637-45 (1995).
Moore et al., “Molecular Mimicry in Protein Synthesis?”,Science, 270:1453-4 (1995).
Bilgin et al., “Solution Structure of the Ternary Complex between Aminoacyl-tRNA, Elongation Factor Tu, and Guanosine Triphosphate”,Biochemistry, 37:8163-72 (1998).
Liljas, A.M., “Ribosomal proteins and elongation factors”,Curr. Opin. Struct. Biol., 5:721-7 (1995).
Negrutskii et al., “Eukaryotic Translation Elongation Factor 1α: Structure, Expression, Functions, and Possible Role in Aminoacyl-tRNA Channeling”,Prog. Nucleic Res. Mol. Biol., 60:47-78 (1998).
Krab et al., “EF-Tu, a GTPase odyssey”,Biochim Biophysics Acta, 1443: 1-22 (1998).
Clark, J., “The ternary complex of EF-Tu and its role in protein biosynthesis”,Curr. Opin. Struct. Biol., 7:110-6 (1997).
Schmitt et al., “Molecular recognition governing the initiation of translation inEscherichia coli. A review”,Biochimie, 78:543-54 (1996).
Cai et al., “Interaction of Mitochondrial Elongation Factor Tu with Aminoacyl-tRNA and Elongation Factor Ts”,J. Biol. Chem., 275:20308-14 (2000).
Nissan et al., “The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA”,Structure Fold Des., 7:143-56 (1999).
Liu et al., “F-actin Sequesters Elongation Factor 1α from Interaction with Aminoacyl-tRNA in a pH-dependent Reaction”,J. Cell. Biol., 135:953-63 (1996).
Reshetnikova et al., “Crystals of Intact Elongation Factor Tu fromThermus themophilusDiffracting to High Resolution”,J. Mol. Biol., 221:375-7 (1991).
Wagner et al., “Interaction of Guanosine Nucleotides and Their Analogs with Elongation Factor Tu fromThermus thermophilus”, 34:12535

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