Purification of inclusion body-forming peptides and proteins in soluble form by fusion to Escherichia coli thermostable proteins.
Proteins and peptides expressed in the prokaryotic system often form inclusion bodies. Solubilization and refolding procedures can be used for their recovery, but this process remains difficult. One strategy for improving the solubility of a protein of interest is to fuse it to a highly soluble protein. To select a suitable fusion partner capable of solubilizing the aggregation-prone (inclusion body-forming) proteins and peptides, Escherichia coli thermostable proteins were identified and tested. Among them, trigger factor (TF) protein was selected because of its high expression and stability. Using an expression system based on fusion to TF, selected proteins and peptides that otherwise form inclusion bodies were expressed in soluble state and were purified like other soluble proteins. This system provides a convenient method for production of aggregation-prone proteins and peptides.
Thapa
Arjun
A
Chosun University, Gwanju, Republic of Korea.
Shahnawaz
Md
M
Karki
Pratap
P
Raj Dahal
Giri
G
Sharoar
Md Golam
MG
Yub Shin
Song
S
Sup Lee
Jung
J
Cho
Byungyun
B
Park
Il-Seon
IS
D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D002479:Inclusion Bodies / Q000378:metabolism*; D010455:Peptides / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification* / Q000378:metabolism*; D012995:Solubility; D013696:Temperature
D029968:Escherichia coli Proteins; D010455:Peptides; D011993:Recombinant Fusion Proteins