High-level synthesis of the 12-kDa human FK506-binding protein in Escherichia coli using translational coupling

Gene ◽  
1993 ◽  
Vol 128 (2) ◽  
pp. 219-225 ◽  
Author(s):  
Tami J. Pilot-Matias ◽  
Steven D. Pratt ◽  
Benjamin C. Lane
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
High Level Synthesis ◽  
Translational Coupling ◽  
Fk506 Binding Protein ◽  
High Level

High-level synthesis of endochitinase ChiA74 in Escherichia coli K12 and its promising potential for use in biotechnology

2013 ◽  
Vol 58 (6) ◽  
pp. 455-462 ◽  
Author(s):  
J. Cristóbal Castañeda-Ramírez ◽  
Norma M. de la Fuente-Salcido ◽  
Rubén Salcedo-Hernández ◽  
Fabiola León-Galván ◽  
Dennis K. Bideshi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Level Synthesis ◽  
Escherichia Coli K12 ◽  
High Level

High-level production of aquaporin Z in Escherichia coli using maltose-binding protein/polyhistidine dual-affinity tag fusion system

2016 ◽  
Vol 51 (5) ◽  
pp. 599-606 ◽  
Author(s):  
Baojian Hang ◽  
Jianfeng Pan ◽  
Desheng Ni ◽  
Qiang Zheng ◽  
Xu Zhang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Fusion System ◽  
Affinity Tag ◽  
Aquaporin Z ◽  
High Level ◽  
Level Production

scholarly journals FK506 Binding Protein from the Hyperthermophilic Archaeon Pyrococcus horikoshii Suppresses the Aggregation of Proteins in Escherichia coli

2002 ◽  
Vol 68 (2) ◽  
pp. 464-469 ◽  
Author(s):  
Akira Ideno ◽  
Masahiro Furutani ◽  
Yoshitaka Iba ◽  
Yoshikazu Kurosawa ◽  
Tadashi Maruyama
Keyword(s):  
Escherichia Coli ◽  
Protein Folding ◽  
Binding Protein ◽  
Fab Fragment ◽  
Ppiase Activity ◽  
Pyrococcus Horikoshii ◽  
E Coli ◽  
Fk506 Binding Protein ◽  
Soluble Recombinant Protein

ABSTRACT The 29-kDa FK506 binding protein (FKBP) gene is the only peptidyl-prolyl cis-trans isomerase (PPIase) gene in the genome of Pyrococcus horikoshii. We characterized the function of this FKBP (PhFKBP29) and used it to increase the production yield of soluble recombinant protein in Escherichia coli. The PPIase activity (k cat/Km ) of PhFKBP29 was found to be much lower than that of other archaeal 16- to 18-kDa FKBPs by a chymotrypsin-coupled assay of the oligo-peptidyl substrate at 15�C. Besides this low PPIase activity, PhFKBP29 showed chaperone-like protein folding activity which enhanced the refolding yield of chemically unfolded rhodanese in vitro. In addition, it suppressed thermal protein aggregation in a temperature range of 45 to 100�C. When the PhFKBP29 gene was coexpressed with the recombinant Fab fragment gene of the anti-hen egg lysozyme antibody in the cytoplasm of E. coli, whose expressed product tended to form an inactive aggregate in E. coli, it improved the yield of the soluble Fab fragments with antibody specificity. PhFKBP29 exerted protein folding and aggregation suppression in E. coli cells.

Expression of foreign proteins in Escherichia coli by fusing with an archaeal FK506 binding protein

2004 ◽  
Vol 64 (1) ◽  
pp. 99-105 ◽  
Author(s):  
A. Ideno ◽  
M. Furutani ◽  
T. Iwabuchi ◽  
T. Iida ◽  
Y. Iba ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Fk506 Binding Protein ◽  
Foreign Proteins
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