skip to main content
DOE Patents title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Methods for production of proteins in host cells

Abstract

The present invention provides methods for the production of proteins, particularly toxic proteins, in host cells. The invention provides methods which use a fusion protein comprising a chaperonin binding domain in host cells induced or regulated to have increased levels of chaperonin which binds the chaperonin binding domain.

Inventors:
;
Issue Date:
Research Org.:
Genecor International, Inc., Rochester, NY (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1174681
Patent Number(s):
6677139
Application Number:
09/470,830
Assignee:
Genecor International, Inc. (Rochester, NY)
Patent Classifications (CPCs):
C - CHEMISTRY C12 - BIOCHEMISTRY C12N - MICROORGANISMS OR ENZYMES
DOE Contract Number:  
W-31-198-ENG-38
Resource Type:
Patent
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Donnelly, Mark, and Joachimiak, Andrzej. Methods for production of proteins in host cells. United States: N. p., 2004. Web.
Donnelly, Mark, & Joachimiak, Andrzej. Methods for production of proteins in host cells. United States.
Donnelly, Mark, and Joachimiak, Andrzej. Tue . "Methods for production of proteins in host cells". United States. https://www.osti.gov/servlets/purl/1174681.
@article{osti_1174681,
title = {Methods for production of proteins in host cells},
author = {Donnelly, Mark and Joachimiak, Andrzej},
abstractNote = {The present invention provides methods for the production of proteins, particularly toxic proteins, in host cells. The invention provides methods which use a fusion protein comprising a chaperonin binding domain in host cells induced or regulated to have increased levels of chaperonin which binds the chaperonin binding domain.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {2004},
month = {1}
}

Patent:

Save / Share:

Works referenced in this record:

Increased solubility of trimethoprim-resistant type SI DHFR from Staphylococcus aureus in Escherichia coli cells overproducing the chaperonins GroEL and GroES
journal, January 1994


Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death
journal, August 1993


Characterization of a functionally important mobile domain of GroES
journal, July 1993


Overexpression of aRhizopus delemar lipase gene inEscherichia coli
journal, February 1993


GFP:HIV-1 Protease Production and Packaging with a T4 Phage Expression-Packaging Processing System
journal, December 1998


Heat shock proteins functioning as molecular chaperones: their roles in normal and stressed cells
book, January 1993


Model Peptide Studies Demonstrate That Amphipathic Secondary Structures Can Be Recognized by the Chaperonin GroEL (cpn60)
journal, February 1997


Interplay of structure and disorder in cochaperonin mobile loops.
journal, October 1996


Different conformations for the same polypeptide bound to chaperones DnaK and GroEL
journal, January 1992


Divergent Effects of Chaperone Overexpression and Ethanol Supplementation on Inclusion Body Formation in RecombinantEscherichia coli
journal, December 1997


The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
journal, January 1996


Protein folding in the central cavity of the GroEL–GroES chaperonin complex
journal, February 1996


Molecular chaperones in protein folding and translocation
journal, February 1996


Homologous plant and bacterial proteins chaperone oligomeric protein assembly
journal, May 1988


Molecular chaperones in cellular protein folding
journal, February 1995


Overproduction of a Functional Fatty Acid Biosynthetic Enzyme Blocks Fatty Acid Synthesis inEscherichia coli
journal, September 1998


Refolding and release of tubulins by a functional immobilized groEL column
journal, September 1994


Synergistic induction of the heat shock response in Escherichia coli by simultaneous treatment with chemical inducers.
journal, January 1995


A structural model for GroEL-polypeptide recognition
journal, April 1997


Refolding chromatography with immobilized mini-chaperones
journal, April 1997


Production of MBP(maltose binding protein)-GroES fusion protein and utilization to stimulate GroEL-mediated protein refolding
journal, January 1998


Expression of correctly folded proteins in Escherichia coli
journal, April 1996


Pseudomonas lipases: Biochemical properties and molecular cloning
journal, August 1993


Analysis of the induction of general stress proteins of Bacillus subtilis
journal, April 1994


Protein Misfolding and Inclusion Body Formation in Recombinant Escherichia coli Cells Overexpressing Heat-shock Proteins
journal, May 1996