Functional display of Pseudomonas and Burkholderia lipases using a translocator domain of EstA autotransporter on the cell surface of Escherichia coli.
Functional expression of the industrially important Pseudomonas and Burkholderia lipases, such as those from P. aeruginosa, B. cepacia and P. fluorescens, was achieved on the cell surface of Escherichia coli using the C-terminal translocator moiety (EstATu) of autotransporter protein (EstA) from P. putida. In particular, lipases which required a lipase-specific foldase (Lif) for their proper folding were for the first time displayed in the active form by coexpression of the Lif protein.
Yang
Taek Ho
TH
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 373-1 Guseong-dong, Daejeon 305-701, Republic of Korea.
Kwon
Min-A
MA
Song
Jae Kwang
JK
Pan
Jae Gu
JG
Rhee
Joon Shick
JS
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D019117:Burkholderia / Q000201:enzymology* / Q000235:genetics; D002265:Carboxylic Ester Hydrolases / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D004926:Escherichia coli / Q000502:physiology*; D008049:Lipase / Q000235:genetics / Q000378:metabolism*; D015202:Protein Engineering / Q000379:methods*; D017434:Protein Structure, Tertiary; D011549:Pseudomonas / Q000201:enzymology* / Q000235:genetics
D001426:Bacterial Proteins; D002265:Carboxylic Ester Hydrolases; C098953:EstA protein, bacteria; D008049:Lipase