DnaK-Mediated Alterations in Human Growth Hormone Protein Inclusion Bodies
- 1 March 1992
- journal article
- research article
- Published by Springer Nature in Nature Biotechnology
- Vol. 10 (3) , 301-304
- https://doi.org/10.1038/nbt0392-301
Abstract
Protein overproduction in microbes frequently results in protein misfolding and aggregation though the molecular basis for this process is unclear. The HSP70 chaperonin, DnaK, was identified as an important factor controlling heterologous protein aggregation in Escherichia coli. Co-overproduction of DnaK significantly reduced human growth hormone (HGH) protein inclusion body formation and the extent of HGH aggregation.Keywords
This publication has 22 references indexed in Scilit:
- The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent mannerCell, 1990
- Renaturation of denatured λ repressor requires heat shock proteinsCell, 1990
- Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cellsCell, 1989
- GENETIC BASIS OF STARVATION SURVIVAL IN NONDIFFERENTIATING BACTERIAAnnual Review of Microbiology, 1989
- Immunogenicity of proteins administered to humans for therapeutic purposesTrends in Biotechnology, 1989
- New Genetic Methods for Mammalian CellsBio/Technology, 1988
- A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptidesNature, 1988
- Speculations on the functions of the major heat shock and glucose-regulated proteinsCell, 1986
- Cytoplasmic Inclusion Bodies in Escherichia coli Producing Biosynthetic Human Insulin ProteinsScience, 1982
- Direct expression in Escherichia coli of a DNA sequence coding for human growth hormoneNature, 1979