Fluorescent proteins from aquatic species

Details Fluorescent proteins from aquatic species Fluorescent proteins from aquatic species

2007-11-06

2007-11-06

Robinson, Hope (Department: 1652)

Chemistry: natural resins or derivatives; peptides or proteins;

Proteins, i.e., more than 100 amino acid residues

C435S069100, C435S006120, C435S252000, C435S320100, C530S300000, C530S350000, C536S023100

Reexamination Certificate

active

11021014

ABSTRACT:
Provided are four new fluorescent proteins. The proteins were derived from two wild-type fluorescent proteins: a red fluorescent protein (RFP) that was isolated fromActinodiscusorDiscosomasp. 1 and a green fluorescent protein (GFP) isolated fromMontastraea cavernosa. Two mutant forms were generated from each wild-type protein. Each of the mutated forms has a higher fluorescence intensity than the respective wild-type form. The mutant forms of the fluorescent proteins allow for more sensitive detection of the fluorescence emitted by the proteins. Additionally, one of the mutant proteins is more resistant to photobleaching than its wild-type protein. The invention also encompasses isolated nucleic acids encoding the mutant forms of the wild-type RFP and GFP.

REFERENCES:
patent: 4968613 (1990-11-01), Masuda
patent: 5096825 (1992-03-01), Barr
patent: 5182202 (1993-01-01), Kajiyama
patent: 5219737 (1993-06-01), Kajiyama
patent: 5229285 (1993-07-01), Kajiyama
patent: 5283179 (1994-02-01), Wood
patent: 5292658 (1994-03-01), Cormier
patent: 5330906 (1994-07-01), Kajiyama
patent: 5352598 (1994-10-01), Kajiyama
patent: 5418155 (1995-05-01), Cormier
patent: 5583024 (1996-12-01), McElroy
patent: 5604123 (1997-02-01), Kazami
patent: 5641641 (1997-06-01), Wood
patent: 5650289 (1997-07-01), Wood
patent: 5670356 (1997-09-01), Sherf et al.
patent: 5674713 (1997-10-01), McElroy
patent: 5700673 (1997-12-01), McElroy
patent: 5744320 (1998-04-01), Sherf
patent: 5786464 (1998-07-01), Seed
patent: 5795737 (1998-08-01), Seed et al.
patent: 5874304 (1999-02-01), Zolotukhin et al.
patent: 5952547 (1999-09-01), Cornelissen et al.
patent: 5968750 (1999-10-01), Zolotukhin
patent: 5976796 (1999-11-01), Szalay
patent: 6020192 (2000-02-01), Muzyczka
patent: 6074859 (2000-06-01), Hirokawa
patent: 6169232 (2001-01-01), Hey et al.
patent: 6342379 (2002-01-01), Tsien et al.
patent: 6414119 (2002-07-01), Fisher
patent: 6689391 (2004-02-01), Goswami et al.
patent: 6723537 (2004-04-01), Peelle
patent: 6900304 (2005-05-01), Tsien et al.
patent: 2002/0064842 (2002-05-01), Sorge et al.
patent: 2002/0107362 (2002-08-01), Thastrup et al.
patent: 2003/0106078 (2003-06-01), Falkowski et al.
patent: 2003/0157643 (2003-08-01), Almond et al.
patent: 2005/0032085 (2005-02-01), Labas et al.
patent: 95/25798 (1995-09-01), None
patent: 96/22376 (1996-07-01), None
patent: 97/26366 (1997-07-01), None
patent: WO 97/28261 (1997-08-01), None
patent: 97/47358 (1997-12-01), None
patent: 99/14336 (1999-03-01), None
patent: WO 00/34526 (2000-06-01), None
patent: WO 01/27150 (2001-04-01), None
patent: WO 01/62919 (2001-08-01), None
patent: WO 02/16944 (2002-02-01), None
patent: WO 02/094992 (2002-11-01), None
patent: WO 03/042401 (2003-05-01), None
patent: WO 03/042401 (2003-05-01), None
Fradkov et al., FEBS Letters, vol. 479, pp. 127-130, 2000.
Seffernick et al., J. Bacteriology, vol. 183, pp. 2405-2410, 2001.
Wells, Biochemistry, vol. 29, pp. 8509-8517, 1990.
GenBank Accession No. AF401282. (Aug. 2001).
Pan W. et al “Vaccine Candidate MSP-I from Plasmodium Falciparum: a Redesigned 4917 bp Polynucleotide Enables Synthesis and Isolation of Full-Length Protein fromEscherichia coliand Mammalian Cells,” Nuc. Acids Res., vol. 27, No. 4, 1094-1103 (1999).
Andrews, “Hierarchy of polyadenylation site usage by bovine papillomavirus in transformed mouse cells,” J. Virology, (1993) p. 7705-7710, 67(12).
Benzakour, “Evaluation of the use of the luciferase-reporter-gene system for gene-regulation studies . . . ” Charter Molecular Genetics Lab (1995), p. 385-387.
Cameron, “Recent advances in transgenic technology,” Molecular Biotechnology (1997, p. 253-265, v. 7.
Chen, “Gene transfer and expression in oligodendrocytes under the control of myelin basic protein transcriptional control region . . . ” Gene Therapy (1998), p. 50-58, v. 5.
Coker, “8-Br-cAMP inhibits the transient expression of firefly luciferase,” FEBS Letters (1989), p. 183-84, v. 249(2).
Faisst, “Compilation of vertebrate-encoded transcription factors,” Nucleic Acids Research (1992), p. 3-26, v. 20(1).
GENBANK AY037770, Montastraea cavernosa green fluorescent protein mRNA (2001).
GENBANK AY056460,Montastraea cavernosacyan fluorescent protein mRNA (2001).
Glass, “Gene functions:E. coliand its heritable elements,” RNA and Protein Productions (1982), p. 95, U. California Press.
Gruber, “Design strategy for synthetic luciferase reporter genes,” 11th Symposium on Bioluminescence & Chemiluminescence (2000), abstract.
Henning, “Humanizing the yeast telomerase template,” Proc. Natl. Acad. Science (1998), p. 5667-5671, v. 95, USA.
Hsieh, “Nucleotide sequence, transcriptional analysis, and glucose regulation of the phenoxazinone synthase gene (phsA) . . . ,” J. Bacteriology (1995), p. 5740-5747, 177(2).
Jensen, “The sequence of spacers between the consensus sequences modulates the strength of prokaryotic promoters,” Applied. and Environmental. Microbiology (1998), p. 82-87, 64(1).
Kappel, “Regulating gene expression in transgenic animals,” Current Opinions in Biotechnology (1992), p. 548-553, v. 3.
Kimura, “Detailed analysis of the mouse H-2Kb promoter: enhancer-like sequences and their role in the regulation of class I gene expression,” Cell (1986), p. 261-272, v. 44.
Kozak, “An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs,” Nucleic Acids Research (1987), p. 8125-8132, 15(20).
Labas, “Diversity and evolution of the green fluorescent protein family,” PNAS (2002), p. 4256-4261, 99(7).
Liu, “Improved assay sensitivity of an engineered secreted Renilla luciferase,” Gene (1999), p. 153-159, v. 237.
Lodish, “Spliceosomes, assembled from snRNPs and a Pre-mRNA, carry out splicing,” Molecular Cell Biology (2000) p. 416-418.
Mount, “Genomic sequence, splicing, and gene annotation,” Am. J. Human Genetics (2000), p. 788-792, v. 67.
Mullins, John J., “Transgenesis in nonmurine species,” Hypertension (1993), p. 630-633, 22(4).
Mullins, Linda, “Molecular medicine in genetically engineered animals,” J. Clin. Invest. (1996) p. 1157-1560, 97(7).
Murray, “Codon usage in plant genes,” Nucleic Acids Research (1988) p. 477-498, 17(2).
Peers, “Regulatory elements controlling pituitary-specific expression of the human prolactin gene,” Molecular and Cellular Biology (1990) p. 4690-4700, v. 10.
Quandt, “Matlnd and Malnspector: new fast and versatile tools for detection of consensus matches in nucleotide sequence data,” Nucleic Acids Research (1995) p. 4878-4884, 23(23).
Ringquist, “Translation initiation inEscherichia coli: sequences within the ribosome-binding site,” Molecular Microbiology (1992) p. 1219-1229, 6(9).
Sala-Newby, “Engineering firefly luciferase as an indicator of cyclic AMP-dependent protein kinase in living cells,” FEBS Letters (1992), p. 241-244, 307(2).
Schatt, “A single DNA-binding transcription factor is sufficient for activation from a distant enhancer and/or from a promoter position,” The EMBO J. (1990) p. 481-487, 9(2).
Seffernick, “Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but functionally different,” J. of Bacteriology (2001) p. 2404-2410, 183(8).
Sharp, “Codon usage patterns inEscherichia coli, Bacillus subtilis, . . . ”, Nucleic Acids Research (1988) p. 8207-8211, 16(17).
Sharp, “The codon adaptation index-a measure of directional synonymous codon usage bias . . . ”, Nucleic Acids Research (1987) p. 1281-1294, 15(3).
Sherf, “Firefly luciferase engineered for improved genetic reporting,” PNotes Magazine (1994), p. 14(8 pages), No. 49, Promega Corporation, Madison, Wisconsin.
Tabaska, “Detection of polyadenylation signals in human DNA sequences,” Gene (1999) p. 77-86, 231.
Viviani, “Bio

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