Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving antigen-antibody binding – specific binding protein...
Patent
1996-12-05
1999-03-02
Wax, Robert A.
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving antigen-antibody binding, specific binding protein...
435 772, 435 23, 435219, 435220, 435221, 435222, 435223, G01N 3353, C12N 950, C12N 952, C12Q 137
Patent
active
058769455
ABSTRACT:
D1 protease has been isolated from the alga (Scenedesmjus obliquus), wheat, and Synechocystis PCC 6803 and the genes encoding these enzymes have been cloned and sequenced. Native or recombinantly produced enzyme has been used to develop assays to detect herbicidal compositions capable of inhibiting the D1 protease enzyme.
REFERENCES:
Satoh, K. Isolated and Properties of the Photosystem II Reaction Center, The Photosynthetic Reaction Center, vol. I, pp. 289-318 (1993).
Seibert, M., Biochemical, Biophysical, and Structural Characterization of the Isolated Photosystem II Reaction Center Complex. Deisenhofer, J. and Norris, J.R., eds. The Photosynthetic Reaction Center, Academic Press, New York, vol. I, pp. 319-356 (1993).
Grebanier, A.E. et al., Membrane Proteins Synthesized but not processed by Isolated Maize Chloroplasts, J. Cell Biol., 78, pp. 734-746 (1978).
Reisfeld et al., Processing of a Chloroplast-Translated Membrane Protein in vivo, Analysis of the Rapidly Synthesized 32000-dalton Shield Protein and Its Precursor in Spirodela oligorrhiza, Dept of Plant Genetics, The Weismann Institute of Science, Rehovot, Eur. J. Biochem. 124, pp. 125-129 (1982).
Minami, J.B. and Watanabe, Detection of a Precursor Polypeptide of the Rapidly-Synthesized 32,000-Dalton Thylakoid Protein in Spinach Chloroplasts, A. Plant. Cell Physiol. 26, pp. 839-846 (1985).
Marder, J.B. et al., Molecular Architecture of the Rapidly Metabolized 32-kilodalton Protein of Photosystem II, J. Biol. Chem. 259, 3900-3908 (1984).
Diner, B.A. et al., COOH-terminal Processing of polypeptide D1 of the photosystem II reaction center of scenedesmus obiquus is necessary for the assembly of the oxygen-evolving complex., 263, pp. 8972-8980 (1988).
Nixon, P.J., Trost, J.T. and Diner, B.A., Role of the Carboxy 'Terminus of Polypeptide D1 in the Assembly of a Functional Water-Oxidizing Manganese Cluster in Photosystem II of the Cyanobacterium Synechocystis sp. PCC 6803: Assembly Requires a Free Carboxyl Group at C-Terminal Position 344; Biochemistry 31: pp. 10859-10870 (1992).
Takahashi et al., COOH-terminal residues of D1 and the 44 kDa Cpa-2 at spinach photosystem II core complex, Febs Lett. 06485 vol. 240, Nos. 1, 2, pp. 6-8 (1988).
Takahashi et al., Chromatographic Purification and Determination of the Carboxy-Terminal Sequences of Photosystem II Reaction Center Proteins, D1 and D2, Plant Cell Physiol., 31, 273-280 (1990).
Taylor, M.A. et al., Characterization of the D1 protein in a photosystem II mutant (LF-1) of scenedesmus obliquus blocked on the oxidizing side. Evident supporting non-processing of D1 as the casue of the lesion, Febs Letters 235: pp. 109-116 (1988).
Shestakov, S.V. et al., Molecular Cloning and Characterization of the ctpA Gene Encoding a Carboxyl-terminal Processing Protease, Journal of Biological Chemistry 269: pp. 1-6 (1994).
Anbudurai, P.R. et al., The ctpA gene encodes the C-terminal processing protease for the D1 protein of the photosystem II reaction center complex, Proceedings of the National Science, USA,, 91, pp. 8082-8086 (1994).
Fujita, S. et al., Identification of the Carboxyl-Terminal Processing Protease for the D1 Precusor Protein of the Photosystem II Reaction Center of Spinach, Plant Cell Physiol., 36(7), 1169-1177 (1995).
Inagaki, N. et al., Carboxyl-terminal processing protease for the D1 precursor protein: cloning and sequening of the spnach cDNA, Plant Molecular Biology 30 pp: 39-50 (1996).
Taguchi et al., Recognition of the Structure around the Site of Cleavage by the Carboxyl-terminal Processing Protease for D1 Precursor Protein of the Photosystem II Reaction Center, J. Biol. Chem., 270(18), pp.: 10711-10716 (1995).
Packer et al., Curr. Res. Photosynth., Proc. Int. Conf. Photosynth., 8th (1990), Meeting Date 1989, vol. III.13, pp. 759-762. Editor(s): Baltscheffsky, Margareta. Publisher: Kluwer, Dordrecht, Netherlands.
Magnin et al., Preliminary Steps in the Purification of the Photosystem II D1 Protein Processing Protease from Maize, Res. Photosynth., Proc. Int. Congr. Photosynth., 9th (1992), vol. II, pp.: 211-214: Editor(s): Murata, N. Publisher: Kluwer, Dordrecht, Netherlands (1992).
Siber, K.R. et al., Tsp: A tail-specific protease that selectively degrades proteins with nonpolar C termini. Proceedings of the National Science, USA, 89: pp. 295-299 (1992).
Hara et al., Cloning, Mapping, and Characterization of the Escherichia coli prc Gene, Which is Involved in C-Terminal Processing of Penicillin-Binding Protein 3, J. Bacteriol. vol. 173, No. 15, pp. 4799-4813 (1991).
Hunt, A. P., Hussey and J. Bowyer, The Production of Trucated Substrates for the D1 processing protease of Photosystem II, Research in Photosynthesis, N. Murata, Editor; Kluwer Academic,Publisher, pp. 207-210 (1992).
Keiler, K.C. and Sauer, R.T., Identification of Active Site Residues of the Tsp Protease, Journal of Biological Chemistry, vol. 270, No. 48: pp.: 28864-28868 (1996).
Oelmuller, R. et al., Molecular Studies of ctpA, the Carboxyl-terminal Processing Protease for the D1 Protein of the Photosystem II Reaction Center in Higher Plants, Journal of Biological Chemistry vol. 271, No. 36, pp.: 21848-21852 (1996).
Pakrasi, H.B. et al., Molecular Analysis of ctpA, the Carboxyl-terminal Processing Protease for the D1 protein of Photosystem II, in Higher Plants and Cyanobacteria, Photosynthesis: from Light to Biosphere, Kluwer Academic Publishers, pp.: 719-724 (1995).
Bowyer, J.R. et al., Carboxyl-terminal Processing of the D1 Protein and Photoactivation of Water-splitting in Photosytem II., Journal of Biological Chemistry, 267, pp.: 5424-5433 (1992).
Fujita, S. et al., Cleavage of a synthetic COOH-terminal oligopeptide of D1 precursor protein by a purified processing enzyme., Febs Letters, 225, pp.: 1-4 (1989).
Inagaki, N., Fujita, S. and Satoh, K., Solubilization and partial purification of a thylakoidal enzyme of spinach involved in the processing of D1 protein, Febs Letters, 246: pp.: 218-222 (1989).
Inagaki, N., Fujita, S. and Satoh, K., Purification and properties of a thylakoidal enzyme of spinach involved in the processing of D1 protein of PS II reaction center, Current research in photosynthesis, M. Baltsvhffsky, Editor, Kluwer Academic Publisher: vol. III, pp.: 763-766 (1990).
Inagaki, N. et al., Carboxyl-terminal processing protease for D1 precursor protein in spinach in Photosynthesis: from light to biosphere, P. Mathis, Editor, Kluwer Academic Publishers: vol. III, pp.:783-786 (I995).
Keiler, K.C., Waller, P.R.H. and Sauer, R.T., Role of a Peptide Tagging System in Degradation of Proteins Synthesized from Damaged Messenger RNA, Science 271: pp.: 990-993 (1996).
Silber, K.R., Sauer, R.T., Deletionof the prc (tsp) gene provides evidence for additional tail-specific proteolytic activity in Escherichia coli K-12, Mol. Gen. Genet 242: pp.: 237-240 (1994).
Taguchi, F. et al., Recognition signal for the C-terminal processing protease of D1 precursor protein in the photosystem II reaction center, Febs Letters 326: pp.: 227-231 (1993).
Takahashi, Y. et al., Genetic engineering of the processing site of D1 precursor protein of photosystem II reaction center in Chlamydomonas reinhardtii, Plant Cell Physiology 37: pp.: 161-168 (1996).
Taylor, M.A., Parker, J.C.L. and Bowyer, J.R., Processing of the D1 polypeptide of the photosystem II reaction center and photoactivation of a low fluorescence mutant (LF-1) of Scenedesmus obliquus, Febs Letters 237: pp.: 229-233 (1988).
Molecular Probes (Eugene, OR 97402-0469) Product Information Sheet for Atto-Tag CBQCA, Feb. 1998.
Chisholm Dexter Allan
Diner Bruce Aaron
Donaldson Gail K.
Hershey Howard Paul
Jordan Douglas Brian
E. I. Du Pont de Nemours and Company
Stole Einar
Wax Robert A.
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