Heterologous protein production using the twin arginine...

Details Heterologous protein production using the twin arginine... Heterologous protein production using the twin arginine...

2003-03-17

2008-11-04

Borin, Michael (Department: 1631)

Data processing: measuring, calibrating, or testing

Measurement system in a specific environment

Biological or biochemical

C703S011000, C435S007100, C530S330000, C530S350000

Reexamination Certificate

active

07447595

ABSTRACT:
Provided are means for evaluating and identifying putative substrates of the twin arginine translocation (Tat) secretory pathway inStreptomycesand other bacterial species. Also provided, therefore, are simple ways to express, secrete and purify correctly folded heterologous proteins on a large scale using host microorganisms, such as,Streptomycesand the Tat pathway therein. Many of the thus-produced proteins are of significant therapeutic value in the pharmaceutical and biochemical industries, particularly when they can be secreted from the host in fully-folded active form. Accordingly, there are further provided the heterologous proteins produced by the Tat secretion pathway using the foregoing methods, and the computer algorithm used to identify the Tat signal sequence and putative substrates.

REFERENCES:
patent: 6022952 (2000-02-01), Weiner et al.
Altschul et al.,J. Molecular Biology, vol. 215, No. 3, pp. 403-410 (Oct. 1990).
Altschul et al., “Gapped BLAST and PSI-BLAST: A New Generation of Protein Database Search Programs,”Nucleic Acids Research, vol. 25, No. 17, pp. 3389-3402, (1997).
Bender et al.,Applied Microbiol. Biotechnol.,vol. 34, Issue 2, pp. 203-207, (1990).
Bentley et al., Complete Genome Sequence of the Model Actinomycete Streptomyces Coelicolor (A3(2)),Nature, vol. 417, pp. 141-147 (2002).
Berks, “A Common Export Pathway for Proteins Binding Complex Redox Cofactors?,”Molecular Microbiology, vol. 22, Issue 3, pp. 393-404 (Nov. 1996).
Berks et al., “The Tat Protein Export Pathway,”Molecular Microbiology, vol. 35, No. 2, pp. 260-274 (2000).
Bogsch et al., “An Essential Component of a Novel Bacterial Protein Export System with Homologues in Plastics and Mitochondria,”J. of Biological Chemisty, vol. 273, No. 29, pp. 18003-18006 (1998).
Brink et al., “Targeting of Thylakoid Proteins by the ΔpH-Driven Twin-Arginine Translocation Pathway Requires a Specific Signal in the Hydrophobic Domain in Conjunction with the Twin-Arginine Motif.”FEBS Letters, vol. 434, pp. 425-430 (1998).
Chaddock et al., “A New Type of Signal Peptide: Central Role of a Twin-Arginine Motif in Transfer Signals for tje ΔpH-Dependent Thylakoidal Protein Translocase”,EMBO J.,vol. 14, pp. 2715-2722 (1995).
Chang et al., In Biology of Actinomycetes '88, “Proc. of Seventh International Symposium on Biology of Actinomycetes”Japanese Sci. Soc. Press, Tokyo, pp. 103-107 (1988).
Cid et al., “Hydrophobicity and Structural Classes in Proteins,”Protein Engineering, vol. 5, No. 5, pp. 373-375, Oxford University Press (1992).
Cline et al., “Transformation of the ArchaebacteriumHalobacterium volcaniiwith Genomic DNA,”J. of Bacteriology, vol. 171, No. 9, pp. 4987-4991, (Sep. 1989).
Cline et al., “Protein-specific Energy Requirements for Protein Transport Across or into Thylakoid Membranes,”J. Biological Chemistry, vol. 267, No. 4, pp. 2688-2696 (1992).
Cristobal et al., “Competition Between Sec- and TAT-Dependent Protein Translocation inEscherichia coli,”The EMBO J.,vol. 18, No. 11, pp. 2982-2990 (1999).
Dilks et al., “Prokaryotic Utilization of the Twin-Arginine Translocation Pathway: a Genomic Survey,”J. Bacteriology, vol. 185, No. 4, pp. 1478-1483 (Feb. 2003).
Engles et al.,Transgenesis—Application of Gene Transfer, (Murray, ed.), Wiley & Sons, pp. 32-53 (1992).
Fekkes et al., “Protein Targeting to the Bacterial Cytoplasmic Membrane,”Microbiology and Molecular Biology Reviews, vol. 63, No. 1, pp. 161-173, (Mar. 1999).
Gilbert et al., “Production and Secretion of Proteins by Streptomyces,”Crit. Rev. Biotechnol.,vol. 15, No. 1, pp. 13-39 (1995).
Hynds et al., “The Sec-Independent Twin-Arginine Translocation System can Transport Both Tightly Folded and Malfolded Proteins Across the Thylakoid Membrane,”J Biological Chemistry, vol. 273, No. 52, pp. 34868-34874 (1998).
Jongbloed et al., “TatC Is a Specificity Determinant for Protein Secretion via the Twin-Arginine Translocation Pathway,”J. Biological Chemistry, vol. 275, No. 52, pp. 41350-41357 (2000).
Kobayashi et al., “Cloning, Expression and Nucleotide Sequence of the α-Amaylase Gene from the Haloalkaliphilic Archaeon Natronococcus sp. Strain Ah-36,”J. Bacteriology, vol. 176, No. 16, pp. 5131-5134 (Aug. 1994).
Matlack et al., “Protein Translocation Tunnel Vision,”Cell, vol. 92, pp. 381-390 (Feb. 1998).
Mori et al., “The Sec Protein-Translocation Pathway,”Trends in Microbiology, vol. 9, Issue 10, pp. 494-500 (Oct. 2001).
Molnar et al., “Recombinant Microbes for Industrial and Agricultural Applicaitons,” (Murooka and Imanaka, eds.) Marcel Dekker, Inc., pp. 81-104 (1994).
Nielsen et al., “Identification of Prokaryotic and Eukaryotic Signal Peptides and Predication of Their Cleavage Sites,”Protein Engineering, vol. 10, No. 1, pp. 1-6 (1997).
Niviere et al., “Site-directed Mutagenesis of the Hydrogenase Signal Peptide Consensus Box Prevents Export of a β-lactamase Fusion Protein,”J. General Microbiology, vol. 138, pp. 2173-2183 (1992).
Noack et al., “Expression and Secretion of Interferon-β1 by Streptomyces lividans: Use of Staphylokinase Signals and Amplification of a Neo Gene,”Gene, vol. 68, Issue 1, pp. 53-62, (Aug. 1988).
Ochsner et al., “Effects of the Twin-Arginine Translocase on Secretion of Virulence Factors, Stress Response, and Pathogenesis,”Proceeding of the National Academy of Sciences of the United States of America, vol. 99, No. 12, pp. 8312-8317 (Jun. 2002).
Pohlschröder et al., “Protein Translocation in the Three Domains of Life: Variations on a Theme,”Cell, vol. 91, pp. 563-566 (Nov. 1997).
Robinson et al., “Protein Targeting by the Twin-Arginine Translocation Pathway,”Nat. Rev. Mol. Cell Biol., vol. 2, No. 5, pp. 350-356 (2001).
Rodrigue et al., “Co-Translocation of a Periplasmic Enzyme Complex by a Hitchhiker Mechanism Through the Bacterial Tat Pathway,”J. Biological Chemistry, vol. 274, No. 19, pp. 13223-13228 (1999).
Rose et al., “Adaptation of Protein Secretion to Extremely High-Salt Conditions by Extensive Use of the Twin-Arginine Translocation Pathway,”Molecular Microbiology, vol. 4, No. 4, pp. 943-950 (2002).
Rowland et al., “The Effect of Signal Sequences on the Efficiency of Secretion of a Heterologous Phosphotriesterase byStreptomyces lividans,”Appl Microbiol. Biotechnol, vol. 38, pp. 94-100 (1992).
Santini et al., “A Novel sec-Independent Periplasmic Protein Translocation Pathway inEscherichia coli,”The EMBO J.,vol. 17, No. 1, pp. 101-112 (1998).
Sargent et al., “Overlapping Functions of Components of a Bacterial Sec-Independent Protein Export Pathway,”The EMBO J.,vol. 17, No. 13, pp. 3640-3650 (1998).
Sargent et al., “Sec-Independent Protein Translocation inEscherichia coli,” J. Biological Chemistry, vol. 274, No. 51, pp. 36073-36082 (1999).
Schaerlaekens et al., “Twin-Arginine Translocation Pathway in Streptomyces lividans,”J Bacteriology, vol. 183, No. 23, pp. 6727-6732 (Dec. 2001).
Settles et al., “Sec-Independent Protein Translocation by the Maize Hcf106 Protein,”Science, vol. 278, pp. 1467-1470 (1997).
Sonnhammer et al., “A Hidden Markov Model for Predicting Transmembrane Helices in Protein Sequences,”Proc. Int. Conf. Intell. Syst. Mol. Biol.,vol. 6, pp. 175-182 (1998).
Stanley et al., “Escherichia coliStrains Blocked in Tat-Dependent Protein Export Exhibit Pleiotropic Defects in the Cell Envelope,”J Bacteriology, vol. 183, No. 1, pp. 139-144 (Jan. 2001).
Thomas, et al., “Export of active Green Fluorescent Protein to the Periplasm by the Twin-Arginine Translocase (Tat) Pathway inEscherichia coli,” Molecular Microbiology, vol. 39, No. 1, pp. 47-53 (2001).
Voelker et al. “Tw

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