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.
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 373-1 Guseong-dong, Daejeon 305-701, Republic of Korea.
Taek Ho
TH
Yang
Min-A
MA
Kwon
Jae Kwang
JK
Song
Jae Gu
JG
Pan
Joon Shick
JS
Rhee
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