Bacterial expression and purification of biologically active mouse c‐Fos proteins by selective codon optimization
Open Access
- 9 June 1997
- journal article
- Published by Wiley in FEBS Letters
- Vol. 409 (2) , 269-272
- https://doi.org/10.1016/s0014-5793(97)00522-x
Abstract
A simple strategy using selective codon optimization was devised to express mouse c‐Fos protein in high levels in E. coli. Ten arginine codons located in the basic region were optimized to achieve high levels of protein expression. The c‐Fos protein was purified to near homogeneity and was demonstrated to be biologically active by assaying its several biological activities.Keywords
This publication has 12 references indexed in Scilit:
- Development of a Sensitive Peptide-Based Immunoassay: Application to Detection of the Jun and Fos OncoproteinsBiochemistry, 1996
- Total synthesis and expression in Escherichia coli of a gene encoding human tropoelastinGene, 1995
- Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli.Genes & Development, 1994
- c-Fos transcriptional activity stimulated by H-Ras-activated protein kinase distinct from JNK and ERKNature, 1994
- JunB differs from c-Jun in its DNA-binding and dimerization domains, and represses c-Jun by formation of inactive heterodimers.Genes & Development, 1993
- [11] Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose platesPublished by Elsevier ,1991
- Codon usage tabulated from the GenBank genetic sequence dataNucleic Acids Research, 1990
- A novel expression vector for high-level synthesis and secretion of foreign proteins in Escherichia coli: overproduction of bovine pancreatic phospholipase A2Gene, 1990
- Detection of fos protein during osteogenesis by monoclonal antibodies.Molecular and Cellular Biology, 1988
- Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genesJournal of Molecular Biology, 1981