Title |
Ubiquitin-like prokaryotic MoaD as a fusion tag for expression of heterologous proteins in Escherichia coli
|
---|---|
Published in |
BMC Biotechnology, January 2014
|
DOI | 10.1186/1472-6750-14-5 |
Pubmed ID | |
Authors |
Sujuan Yuan, Xin Wang, Jian Xu, Zheng Yan, Nan Wang |
Abstract |
Eukaryotic ubiquitin and SUMO are frequently used as tags to enhance the fusion protein expression in microbial host. They increase the solubility and stability, and protect the peptides from proteolytic degradation due to their stable and highly conserved structures. Few of prokaryotic ubiquitin-like proteins was used as fusion tags except ThiS, which enhances the fusion expression, however, reduces the solubility and stability of the expressed peptides in E. coli. Hence, we investigated if MoaD, a conserved small sulfur carrier in prokaryotes with the similar structure of ubiquitin, could also be used as fusion tag in heterologous expression in E. coli. |
X Demographics
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 1 | 100% |
Demographic breakdown
Type | Count | As % |
---|---|---|
Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 21 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 5 | 24% |
Student > Master | 4 | 19% |
Researcher | 4 | 19% |
Student > Bachelor | 2 | 10% |
Lecturer | 1 | 5% |
Other | 3 | 14% |
Unknown | 2 | 10% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 6 | 29% |
Agricultural and Biological Sciences | 5 | 24% |
Chemistry | 3 | 14% |
Pharmacology, Toxicology and Pharmaceutical Science | 1 | 5% |
Computer Science | 1 | 5% |
Other | 3 | 14% |
Unknown | 2 | 10% |