Functional solubilization of aggregation-prone TRAIL protein facilitated by coexpressing with protein isoaspartate methyltranferase.

Abstract

TRAIL was a tumor-specific protein in development as a novel anticancer therapeutic agent. Generally, when expressed in recombinant Escherichia coli, TRAIL protein was prone to form inclusion bodies. In this study, coexpression of human TRAIL protein and protein isoaspartate methyltranferase (PIMT) from E. coli on plasmid pBV-TRAIL-PCM in E. coli C600 was investigated to overcome the difficulties in soluble expression. The results showed that this PIMT coexpression strategy exerted a positive effect on the TRAIL protein expression in recombinant E. coli, which led to a mean increase in the intracellular concentration of soluble and total protein of TRAIL by 1.57-fold and 1.33-fold, respectively. At the same time, results also suggested that PIMT was a prospective partner for soluble expression of TRAIL protein.

• Authors: Hu Zhu, Ruo-Jun Pan, Tian-Wen Wang, Ya-Ling Shen, Dong-Zhi Wei
• Journal: Applied microbiology and biotechnology (Appl Microbiol Biotechnol) Vol. 72 Issue 5 Pg. 1033-8 (Oct 2006) ISSN: 0175-7598 [Print] Germany
• PMID: 16575568 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• TNF-Related Apoptosis-Inducing Ligand
• Protein D-Aspartate-L-Isoaspartate Methyltransferase

Topics

• Cloning, Molecular
• Escherichia coli (genetics, growth & development, metabolism)
• Fermentation
• Protein D-Aspartate-L-Isoaspartate Methyltransferase (biosynthesis, genetics)
• TNF-Related Apoptosis-Inducing Ligand (biosynthesis, genetics)