Enhanced functional expression of aquaporin Z via fusion of in situ cleavable leader peptides in Escherichia coli cell-free system

Enzyme and Microbial Technology

Volumn 55, Issue , 2014, Pages 26-30

  Zhang, Xu ^a   Lian, Jiazhang ^a   Kai, Lei ^a,b   Huang, Lei ^a   Cen, Peilin ^a   Xu, Zhinan ^a  

^a ZHEJIANG UNIVERSITY   (China)

^b GOETHE UNIVERSITY   (Germany)

Author keywords

Aquaporin Z; Cell free protein synthesis; Leader peptidase; Leader peptide; Membrane protein

Indexed keywords

BIOLOGICAL MEMBRANES; BIOMIMETIC PROCESSES; ESCHERICHIA COLI; SOAPS (DETERGENTS); TOBACCO; WATER FILTRATION;

AQUAPORIN Z; CELL FREE PROTEIN SYNTHESIS; ESCHERICHIA COLI CELL-FREE SYSTEMS; FILTRATION TECHNOLOGIES; HYDROPHOBIC ENVIRONMENT; INTEGRAL MEMBRANE PROTEINS; LEADER PEPTIDASE; MEMBRANE PROTEINS;

PEPTIDES;

AQUAPORIN; AQUAPORIN Z; BACTERIAL PROTEIN; DETERGENT; HYBRID PROTEIN; LIPOSOME; MONOMER; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; CELL FREE SYSTEM; ESCHERICHIA COLI; HYDROPHOBICITY; IN VITRO STUDY; LIGHT SCATTERING; NONHUMAN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN SYNTHESIS; WATER TRANSPORT;

AQUAPORIN Z; CELL-FREE PROTEIN SYNTHESIS; LEADER PEPTIDASE; LEADER PEPTIDE; MEMBRANE PROTEIN;

AMINO ACID SEQUENCE; AQUAPORINS; CELL-FREE SYSTEM; DETERGENTS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENES, SYNTHETIC; GENETIC VECTORS; LIPOSOMES; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN BIOSYNTHESIS; PROTEIN SORTING SIGNALS; RECOMBINANT FUSION PROTEINS; SERINE ENDOPEPTIDASES; TRANSCRIPTION, GENETIC; WATER;

EID: 84891751003     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2013.12.002     Document Type: Article

References (25)

1. Swartz J. Developing cell-free biology for industrial applications. J Ind Microbiol Biotechnol 2006, 33:476-485.
2. Lian J., Ding S., Cai J., Zhang D., Xu Z., Wang X. Improving aquaporin Z expression in Escherichia coli by fusion partners and subsequent condition optimization. Appl Microbiol Biotechnol 2009, 82:463-470.
3. Klammt C., Schwarz D., Lohr F., Schneider B., Dotsch V., Bernhard F. Cell-free expression as an emerging technique for the large scale production of integral membrane protein. FEBS J 2006, 273:4141-4153.
4. Klammt C., Schwarz D., Fendler K., Haase W., Dotsch V., Bernhard F. Evaluation of detergents for the soluble expression of α-helical and β-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system. FEBS J 2005, 272:6024-6038.
5. Nomura S.M., Kondoh S., Asayama W., Asada A., Nishikawa S., Akiyoshi K. Direct preparation of giant proteo-liposomes by in vitro membrane protein synthesis. J Biotechnol 2008, 133:190-195.
6. Shimizu Y., Inoue A., Tomari Y., Suzuki T., Yokogawa T., Nishikawa K., et al. Cell-free translation reconstituted with purified components. Nat Biotechnol 2001, 19:751-755.
7. Stenstrom C.M., Holmgren E., Isaksson L.A. Cooperative effects by the initiation codon and its flanking regions on translation initiation. Gene 2001, 273:259-265.
8. Xu Z., Lian J., Cai J. Efficient expression of aquaporin Z in Escherichia coli cell-free system using different fusion vectors. Protein Pept Lett 2010, 17:181-185.
9. Pritchard M.P., Ossetian R., Li D.N., Henderson C.J., Burchell B., Wolf C.R., et al. A general strategy for the expression of recombinant human cytochrome P450s in Escherichia coli using bacterial signal peptides: expression of CYP3A4, CYP2A6, and CYP2E1. Arch Biochem Biophys 1997, 345:342-354.
10. Tschantz W., Paetze M., Cao G., Suciu D., Inouye M., Dalbey R.E. Characterization of a soluble, catalytically active form of Escherichia coli leader peptidase: requirement of detergent or phospholipid for optimal activity. Biochemistry 1995, 34:3935-3941.
11. Choo K.H., Tan T.W., Ranganathan S. SPdb - a signal peptide database. BMC Bioinformatics 2005, 6:249.
12. Kai L., Kaldenhoff R., Lian J., Zhu C., Dötsch V., Bernhard F., et al. Preparative scale production of functional mouse aquaporin 4 using different cell-free expression modes. PLoS ONE 2010, 5:e12972.
13. Borgnia M.J., Kozono D., Calamita G., Maloney P.C., Agre P. Functional reconstitution and characterization of AqpZ, the E. coli water channel protein. J Mol Biol 1999, 291:1169-1179.
14. Hovijitra N.T., Wuu J.J., Peaker B., Swartz J.R. Cell-Free synthesis of functional aquaporin Z in synthetic liposomes. Biotechnol Bioeng 2009, 104:40-49.
15. Pohl P., Saparov S.M., Borgnia M.J., Agre P. Highly selective water channel activity measured by voltage clamp: analysis of planar lipid bilayers reconstituted with purified AqpZ. Proc Natl Acad Sci USA 2001, 98:9624-9629.
16. Kumar M., Grzelakowski M., Zilles J., Clark M., Meier W. Highly permeable polymeric membranes based on the incorporation of the functional water channel protein Aquaporin Z. Proc Natl Acad Sci USA 2007, 104:20719-20724.
17. Berrier C., Park K.H., Abes S., Bibonne A., Betton J.M., Ghazi A. Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent. Biochemistry 2004, 43:12585-12591.
18. Elbaz Y., Steiner-Mordoch S., Danieli T., Schuldiner S. In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state. Proc Natl Acad Sci USA 2004, 101:1519-1524.
19. Klammt C., Schwarz D., Eifler N., Engel A., Piehler J., Haase W., et al. Cell-free production of G protein-coupled receptors for functional and structural studies. J Struct Biol 2007, 158:482-493.
20. Ahn J.H., Hwang M.Y., Lee K.H., Choi C.Y., Kim D.M. Use of signal sequences as an in situ removable sequence element to stimulate protein synthesis in cell-free extracts. Nucleic Acids Res 2007, 35:e21.
21. Stenström C.M., Jin H., Major L.L., Tate W.P., Isaksson L.A. Codon bias at the 3'-side of the initiation codon is correlated with translation initiation efficiency in Escherichia coli. Gene 2001, 263:273-284.
22. Stenström C.M., Isaksson L.A. Influences on translation initiation and early elongation by the messenger RNA region flanking the initiation codon at the 3' side. Gene 2002, 288:1-8.
23. Voges D., Watzele M., Nemetz C., Wizemann S., Buchberger B. Analyzing and enhancing mRNA translational efficiency in an Escherichia coli in vitro expression system. Biochem Biophys Res Commun 2004, 318:601-614.
24. Chen H., Fan L., Xu Z., Yin X., Cen P. Efficient production of soluble beta-defensin-3-4 fusion proteins in Escherichia coli cell-free system. Process Biochem 2007, 42:423-428.
25. Ishihara G., Goto M., Saeki M., Ito K., Hori T., Kigawa T., et al. Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors. Protein Expr Purif 2005, 41:27-37.