Hosts and methods for producing recombinant products in high yie

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Enzymatic production of a protein or polypeptide

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

4351721, 4351723, 435839, 435849, 935 16, 935 72, 935 73, 935 74, C12P 2100, C12N 1500

Patent

active

047585129

DESCRIPTION:

BRIEF SUMMARY
rganisms and methods of this invention permit the large-scale production of foreign recombinant products in high yields.


BRIEF DESCRIPTION OF THE DRAWINGS

FIG. 1 is a table which indicates the level of protease La isolated from htpR mutants at 30.degree. and 42.degree. C.
FIG. 2 is a comparative graphical presentation of the percentage of degradation vs. time for various incomplete E. coli polypeptides that have incorporated puromycin.
FIG. 3 is a comparative graphical presentation of the percentage of degradation vs. time for various abnormal E. coli proteins that contain canavanine in place of arginine.


BEST MODE OF CARRYING OUT THE INVENTION

In order that the invention herein described may be more fully understood, the following detailed description is set forth.
In the description, the following terms are employed:
Nucleotide--A monomeric unit of DNA or RNA consisting of a sugar moiety (pentose), a phosphate, and a nitrogenous heterocyclic base. The base is linked to the sugar moiety via the glycosidic carbon (1' carbon of the pentose) and that combination of base and sugar is called a nucleoside. The base characterizes the nucleotide. The four DNA bases are adenine ("A"), guanine ("G"), cytosine ("C"), and thymine ("T"). The four RNA bases are A, G, C and uracil ("U").
DNA Sequence--A linear array of nucleotides connected one to the other by phosphodiester bonds between the 3' and 5' carbons of adjacent pentoses.
Codon--A DNA sequence of three nucleotides (a triplet) which encodes, through its template or messenger RNA ("mRNA"), an amino acid, a translation start signal or a translation termination signal. For example, the nucleotide triplets TTA, TTG, CTT, CTC, CTA and CTG encode the amino acid leucine ("Leu"), TAG, TAA and TGA are translation stop signals and ATG is a translation start signal.
Polypeptide--A linear array of amino acids connected one to the other by peptide bonds between the .alpha.-amino and carboxy groups of adjacent amino acids.
Gene--A DNA sequence which encodes through its mRNA a sequence of amino acids characteristic of a specific polypeptide.
Transcription--The process of producing mRNA from a gene or DNA sequence.
Translation--The process of producing a polypeptide from mRNA.
Expression--The process of producing a polypeptide from a DNA sequence or gene. It involves transcription and translation.
Plasmid--A nonchromosomal, double-stranded DNA sequence comprising an intact "replicon" such that the plasmid is replicated in a host cell. When the plasmid is placed within a unicellular organism, the characteristics of that organism may be changed or transformed as a result of the DNA of the plasmid. For example, a plasmid carrying the gene for tetracycline resistance (Tet.sup.R) transforms a cell previously sensitive to tetracycline into one which is resistant to it. A host cell transformed by a plasmid or vector is called a "transformant".
Phage or Bacteriophage--Bacterial virus many of which consist of DNA sequences encapsidated in a protein envelope or coat ("capsid").
Cloning Vehicle or Vector--A plasmid, phage DNA or other DNA sequence which is able to replicate in a host cell, characterized by one or a small number of endonuclease recognition or restriction sites at which such DNA sequences may be cut in a determinable fashion without attendant loss of an essential biological function of the DNA, e.g., replication, production of coat proteins or loss of promoter or binding sites, and which contains a marker suitable for use in the identification of transformed cells, e.g., tetracycline resistance or ampicillin resistance.
Cloning--The process of obtaining a population of organisms or DNA sequences derived from one such organism or sequence by asexual reproduction.
Recombinant DNA Molecule or Hybrid DNA--A molecule consisting of segments of DNA from different genomes (the entire DNA of a cell or virus) which have been joined end-to-end outside of living cells and have the capacity to infect some host cell and to be maintained therein.
Expression Control Sequence--A sequ

REFERENCES:
Neidhardt, Van Bogelen and Lau, J. Bacteriol., 153: 597-603, 1983 (Feb.).
Neidhardt and Van Bogelen, Biochem. and Biophys. Res. Comm., 100: 894-900, 1981.
Bachmann, Microbiol. Rev., 47: 180-230, 1983 (Jun.).
T. A. Baker et al., "Proteolysis Defect in htpR Mutants of E. Coli", Abstracts of papers presented at Phage and Bacterial Regulatory Mechanisms, Cold Spring Harbor, New York, p. 87 (Aug. 23-28, 1983).
V. G. Corces et al., "Localization of Sequences Responsible for Heat Shock Induced Transcription", J. Cell. Biochem. Suppl., O(6), p. 340 (1982).
C. H. Chung et al., "The Product of the lon (capR) Gene in Escherichia coli is the ATP-Dependent Protease, Protease La", Proc. Natl. Acad. Sci. USA, 78 (No. 8), pp. 4931-4935 (Aug. 1981).
C. H. Chung et al., "Studies of the Protein Encoded by the lon Mutation, CapR9, in Echerichia coli", J. Biol. Chem., 258 (No. 1), pp. 215-221 (Jan. 10, 1983).
K. E. Davies, "A Comprehensive List of Cloned Eukaryotic Genes", Genetic Engineering, 3, Williamson (ed.), Academic Press, New York, pp. 143-173 (1982).
M. Desautels et al., "Demonstration of an ATP-Dependent, Vanadate-Sensitive Endoprotease in the Matrix of Rat Liver Mitochondria", J. Biol. Chem., 257 (No. 19), pp. 11673-11679 (Oct. 10, 1982).
S. Gottesman et al., "Deg Phenotype of Escherichia coli lon Mutants", J. Bacteriol., 133 (No. 2), pp. 844-851 (Feb. 1978).
A. D. Grossman et al., "Mutations in the lon Gene of E. coli K12 Phenotypically Suppress a Mutation in the Sigma Subunit of RNA Polymerase", Cell, 32, pp. 151-159 (Jan. 1983).
M. Houghton et al., "The Complete Amino Acid Sequence of Human Fibroblast Interferon as Deduced Using Synthetic Oligodeoxyribonucleotide Primers of Reverse Transcriptase", Nucleic Acids Res., 8 (No. 13), pp. 2885-2894 (1980).
D. G. Klapper et al., "Sequence Analysis of Somatomedin-C: Confirmation of Identity with Insulin-Like Growth Factor I", Chemical Abstracts, 99, Abstract No. 48021d (1983), of Endocrinology, 112, pp. 2215-2217 (1983).
J. D. Kowit et al., "Intermediate Steps in the Degradation of a Specific Abnormal Protein in Escherichia coli", J. Biol. Chem., 252 (No. 23), pp. 8350-8357 (Dec. 10, 1977).
F. S. Larimore et al., "Studies of the ATP-Dependent Proteolytic Enzyme, Protease La, From Escherichia coli", J. Biol. Chem., 257 (No. 8), pp. 4187-4195 (Apr. 25, 1982).
S. Lin et al., ".beta.-Galactosidase: Rates of Synthesis and Degradation of Incomplete Chains", J. Biol. Chem., 247 (No. 7), pp. 2205-2211 (Apr. 10, 1972).
F. C. Neidhardt et al., "The High-Temperature Regulon of Escherichia coli", in Heat Shock: From Bacteria to Man, M. J. Schlesinger et al. (ed.), Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, pp. 139-145 (1982).
K. Olden et al., "Studies of the Energy Requirement for Intracellular Protein Degradation in Escherichia coli", Biochim. et Biophys. Acta, 542, pp. 385-398 (1978).
T. M. Roberts et al., "A General Method for Maximizing the Expression of a Cloned Gene", Proc. Natl. Acad. Sci. USA, 76 (No. 2), pp. 760-764 (Feb. 1979).
W. J. Rutter, "Production of `Valuable` Proteins in Alternate Biological Hosts", in Recombinant DNA and Genetic Experimentation, J. Morgan et al., (eds.), Pergamon Press, pp. 123-128 (1979).
B. Shineberg et al., "The lon Gene and Degradation of .beta.-Galactosidase Nonsense Fragments", J. Bacteriol., 116 (No. 3), pp. 1469-1471 (Dec. 1973).
A. St. John et al., "Further Evidence for the Involvement of Charged tRNA and Guanosine Tetraphosphate in the Control of Protein Degradation in Escherichia coli", J. Biol. Chem., 253 (No. 11), pp. 3945-3951 (Jun. 10, 1978).
K. H. S. Swamy et al., "E. Coli Contains Eight Soluble Proteolytic Activities, One Being ATP Dependent", Nature, 292 (No. 5824), pp. 652-654 (Aug. 13, 1981).
K. Tilly et al., "Identification of the Heat-Inducible Protein C15.4 as the groES Gene Product in Escherichia-coli", J. Bacteriol., 154 (No. 3), pp. 1505-1507 (Jun. 1983).
K. Tilly et al., "The dnaK Protein Modulates the Heat-Shock Response of Escherichia coli

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Hosts and methods for producing recombinant products in high yie does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Hosts and methods for producing recombinant products in high yie, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Hosts and methods for producing recombinant products in high yie will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-597000

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.