Premium
The chaperone activity of trigger factor is distinct from its isomerase activity during co‐expression with adenylate kinase in Escherichia coli
Author(s) -
Li Zhen-Yu,
Liu Chuan-Peng,
Zhu Liu-Qin,
Jing Guo-Zhong,
Zhou Jun-Mei
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02896-4
Subject(s) - adenylate kinase , isomerase , escherichia coli , mutant , plasmid , protein disulfide isomerase , chaperone (clinical) , wild type , biochemistry , microbiology and biotechnology , chemistry , inclusion bodies , biology , enzyme , gene , medicine , pathology
To investigate the molecular chaperone function of trigger factor (TF) and its relationship with isomerase activity in vivo, the assisted folding of adenylate kinase (AK) by TF in Escherichia coli was examined by measuring the amounts of soluble AK produced during co‐expression. When the mutant of chicken AK, P17G, is expressed in plasmid pBVAK, 95% of the protein is found in inclusion bodies. Co‐expression of AK with TF was achieved using a plasmid pBVAT that allowed expression of TF and AK in the same plasmid under separate control. Co‐expression with TF resulted in an increase in the amount of soluble AK, with a higher increase when TF was expressed at higher levels in the cell. Co‐expression of AK with the two TF mutants, Y221G and F233Y, in which peptidyl‐prolyl cis / trans isomerase activity was 1% of wild‐type, gave the same results as wild‐type TF. This provides in vivo evidence that the molecular chaperone activity of TF is distinct from its isomerase activity.