메뉴 건너뛰기




Volumn 110, Issue 42, 2013, Pages 16796-16801

In vitro evolution of α-hemolysin using a liposome display

Author keywords

Directed evolution; FACS; Giant unilamellar vesicles; In vitro synthetic biology; Pure system

Indexed keywords

ALPHA HEMOLYSIN; LIGAND; LIPOSOME; MUTANT PROTEIN;

EID: 84885737601     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1314585110     Document Type: Article
Times cited : (119)

References (44)
  • 1
    • 33746695331 scopus 로고    scopus 로고
    • Cell-free expression systems for eukaryotic protein production
    • Endo Y, Sawasaki T (2006) Cell-free expression systems for eukaryotic protein production. Curr Opin Biotechnol 17(4): 373-380.
    • (2006) Curr Opin Biotechnol , vol.17 , Issue.4 , pp. 373-380
    • Endo, Y.1    Sawasaki, T.2
  • 2
    • 84864953230 scopus 로고    scopus 로고
    • Cell-free protein synthesis: Applications come of age
    • Carlson ED, Gan R, Hodgman CE, Jewett MC (2012) Cell-free protein synthesis: Applications come of age. Biotechnol Adv 30(5): 1185-1194.
    • (2012) Biotechnol Adv , vol.30 , Issue.5 , pp. 1185-1194
    • Carlson, E.D.1    Gan, R.2    Hodgman, C.E.3    Jewett, M.C.4
  • 3
    • 33748478328 scopus 로고    scopus 로고
    • In vitro evolution of proteins
    • Matsuura T, Yomo T (2006) In vitro evolution of proteins. J Biosci Bioeng 101(6): 449-456.
    • (2006) J Biosci Bioeng , vol.101 , Issue.6 , pp. 449-456
    • Matsuura, T.1    Yomo, T.2
  • 4
    • 0035424963 scopus 로고    scopus 로고
    • In vitro display technologies: Novel developments and applications
    • Amstutz P, Forrer P, Zahnd C, Plückthun A (2001) In vitro display technologies: Novel developments and applications. Curr Opin Biotechnol 12(4): 400-405.
    • (2001) Curr Opin Biotechnol , vol.12 , Issue.4 , pp. 400-405
    • Amstutz, P.1    Forrer, P.2    Zahnd, C.3    Plückthun, A.4
  • 5
    • 0035810165 scopus 로고    scopus 로고
    • Functional proteins from a random-sequence library
    • Keefe AD, Szostak JW (2001) Functional proteins from a random-sequence library. Nature 410(6829): 715-718.
    • (2001) Nature , vol.410 , Issue.6829 , pp. 715-718
    • Keefe, A.D.1    Szostak, J.W.2
  • 7
    • 0034213573 scopus 로고    scopus 로고
    • Do more complex organisms have a greater proportion of membrane proteins in their genomes?
    • Stevens TJ, Arkin IT (2000) Do more complex organisms have a greater proportion of membrane proteins in their genomes? Proteins 39(4): 417-420.
    • (2000) Proteins , vol.39 , Issue.4 , pp. 417-420
    • Stevens, T.J.1    Arkin, I.T.2
  • 8
    • 84867635731 scopus 로고    scopus 로고
    • Transforming a drug/H+ antiporter into a polyamine importer by a single mutation
    • Brill S, Falk OS, Schuldiner S (2012) Transforming a drug/H+ antiporter into a polyamine importer by a single mutation. Proc Natl Acad Sci USA 109(42): 16894-16899.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.42 , pp. 16894-16899
    • Brill, S.1    Falk, O.S.2    Schuldiner, S.3
  • 9
    • 54449087770 scopus 로고    scopus 로고
    • Directed evolution of a G protein-coupled receptor for expression, stability, and binding selectivity
    • Sarkar CA, et al. (2008) Directed evolution of a G protein-coupled receptor for expression, stability, and binding selectivity. Proc Natl Acad Sci USA 105(39): 14808-14813.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.39 , pp. 14808-14813
    • Sarkar, C.A.1
  • 10
    • 79954569232 scopus 로고    scopus 로고
    • Solubilization of a membrane protein by combinatorial supercharging
    • Hajduczki A, Majumdar S, Fricke M, Brown IA, Weiss GA (2011) Solubilization of a membrane protein by combinatorial supercharging. ACS Chem Biol 6(4): 301-307.
    • (2011) ACS Chem Biol , vol.6 , Issue.4 , pp. 301-307
    • Hajduczki, A.1    Majumdar, S.2    Fricke, M.3    Brown, I.A.4    Weiss, G.A.5
  • 11
    • 84862546176 scopus 로고    scopus 로고
    • Critical Features for Biosynthesis, stability, and functionality of a G protein-coupled receptor uncovered by all-versus-all mutations
    • Schlinkmann KM, et al. (2012) Critical features for biosynthesis, stability, and functionality of a G protein-coupled receptor uncovered by all-versus-all mutations. Proc Natl Acad Sci USA 109(25): 9810-9815.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.25 , pp. 9810-9815
    • Schlinkmann, K.M.1
  • 12
    • 33748759588 scopus 로고    scopus 로고
    • Directed evolution of a bacterial efflux pump: Adaptation of the E coli TolC exit duct to the Pseudomonas MexAB translocase
    • Bokma E, Koronakis E, Lobedanz S, Hughes C, Koronakis V (2006) Directed evolution of a bacterial efflux pump: Adaptation of the E. coli TolC exit duct to the Pseudomonas MexAB translocase. FEBS Lett 580(22): 5339-5343.
    • (2006) FEBS Lett , vol.580 , Issue.22 , pp. 5339-5343
    • Bokma, E.1    Koronakis, E.2    Lobedanz, S.3    Hughes, C.4    Koronakis, V.5
  • 13
    • 84862800120 scopus 로고    scopus 로고
    • A molecular transporter engineering approach to improving xylose catabolism in Saccharomyces cerevisiae
    • Young EM, Comer AD, Huang H, Alper HS (2012) A molecular transporter engineering approach to improving xylose catabolism in Saccharomyces cerevisiae. Metab Eng 14(4): 401-411.
    • (2012) Metab Eng , vol.14 , Issue.4 , pp. 401-411
    • Young, E.M.1    Comer, A.D.2    Huang, H.3    Alper, H.S.4
  • 14
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
    • Song L, et al. (1996) Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 274(5294): 1859-1866.
    • (1996) Science , vol.274 , Issue.5294 , pp. 1859-1866
    • Song, L.1
  • 15
    • 0034904102 scopus 로고    scopus 로고
    • Cell-free translation reconstituted with purified components
    • Shimizu Y, et al. (2001) Cell-free translation reconstituted with purified components. Nat Biotechnol 19(8): 751-755.
    • (2001) Nat Biotechnol , vol.19 , Issue.8 , pp. 751-755
    • Shimizu, Y.1
  • 16
    • 70349908271 scopus 로고    scopus 로고
    • Population analysis of structural properties of giant liposomes by flow cytometry
    • Nishimura K, et al. (2009) Population analysis of structural properties of giant liposomes by flow cytometry. Langmuir 25(18): 10439-10443.
    • (2009) Langmuir , vol.25 , Issue.18 , pp. 10439-10443
    • Nishimura, K.1
  • 17
    • 48049092838 scopus 로고    scopus 로고
    • HaloTag: A novel protein labeling technology for cell imaging and protein analysis
    • Los GV, et al. (2008) HaloTag: A novel protein labeling technology for cell imaging and protein analysis. ACS Chem Biol 3(6): 373-382.
    • (2008) ACS Chem Biol , vol.3 , Issue.6 , pp. 373-382
    • Los, G.V.1
  • 18
    • 0026785678 scopus 로고
    • Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis
    • Walker B, Krishnasastry M, Zorn L, Bayley H (1992) Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis. J Biol Chem 267(30): 21782-21786.
    • (1992) J Biol Chem , vol.267 , Issue.30 , pp. 21782-21786
    • Walker, B.1    Krishnasastry, M.2    Zorn, L.3    Bayley, H.4
  • 19
    • 33748287106 scopus 로고    scopus 로고
    • Femtoliter compartment in liposomes for in vitro selection of proteins
    • Sunami T, et al. (2006) Femtoliter compartment in liposomes for in vitro selection of proteins. Anal Biochem 357(1): 128-136.
    • (2006) Anal Biochem , vol.357 , Issue.1 , pp. 128-136
    • Sunami, T.1
  • 20
    • 84861878032 scopus 로고    scopus 로고
    • Construction of a gene screening system using giant unilamellar liposomes and a fluorescence-activated cell sorter
    • Nishikawa T, Sunami T, Matsuura T, Ichihashi N, Yomo T (2012) Construction of a gene screening system using giant unilamellar liposomes and a fluorescence-activated cell sorter. Anal Chem 84(11): 5017-5024.
    • (2012) Anal Chem , vol.84 , Issue.11 , pp. 5017-5024
    • Nishikawa, T.1    Sunami, T.2    Matsuura, T.3    Ichihashi, N.4    Yomo, T.5
  • 21
    • 84861861133 scopus 로고    scopus 로고
    • Cell-free protein synthesis inside giant unilamellar vesicles analyzed by flow cytometry
    • Nishimura K, et al. (2012) Cell-free protein synthesis inside giant unilamellar vesicles analyzed by flow cytometry. Langmuir 28(22): 8426-8432.
    • (2012) Langmuir , vol.28 , Issue.22 , pp. 8426-8432
    • Nishimura, K.1
  • 22
    • 33748751596 scopus 로고    scopus 로고
    • Evidence that clustered phosphocholine head groups serve as sites for binding and assembly of an oligomeric protein pore
    • Valeva A, et al. (2006) Evidence that clustered phosphocholine head groups serve as sites for binding and assembly of an oligomeric protein pore. J Biol Chem 281(36): 26014-26021.
    • (2006) J Biol Chem , vol.281 , Issue.36 , pp. 26014-26021
    • Valeva, A.1
  • 23
    • 0027241025 scopus 로고
    • Altered pore-forming properties of proteolytically nicked staphylococcal alpha-toxin
    • Palmer M, Weller U, Messner M, Bhakdi S (1993) Altered pore-forming properties of proteolytically nicked staphylococcal alpha-toxin. J Biol Chem 268(16): 11963-11967.
    • (1993) J Biol Chem , vol.268 , Issue.16 , pp. 11963-11967
    • Palmer, M.1    Weller, U.2    Messner, M.3    Bhakdi, S.4
  • 24
    • 67650654611 scopus 로고    scopus 로고
    • Membrane protein expression: No cells required
    • Katzen F, Peterson TC, Kudlicki W (2009) Membrane protein expression: No cells required. Trends Biotechnol 27(8): 455-460.
    • (2009) Trends Biotechnol , vol.27 , Issue.8 , pp. 455-460
    • Katzen, F.1    Peterson, T.C.2    Kudlicki, W.3
  • 25
    • 0037407011 scopus 로고    scopus 로고
    • Arresting and releasing Staphylococcal α-hemolysin at intermediate stages of pore formation by engineered disulfide bonds
    • Kawate T, Gouaux E (2003) Arresting and releasing Staphylococcal α-hemolysin at intermediate stages of pore formation by engineered disulfide bonds. Protein Sci 12(5): 997-1006.
    • (2003) Protein Sci , vol.12 , Issue.5 , pp. 997-1006
    • Kawate, T.1    Gouaux, E.2
  • 26
    • 35348908966 scopus 로고    scopus 로고
    • Bacterial protein secretion through the translocase nanomachine
    • Papanikou E, Karamanou S, Economou A (2007) Bacterial protein secretion through the translocase nanomachine. Nat Rev Microbiol 5(11): 839-851.
    • (2007) Nat Rev Microbiol , vol.5 , Issue.11 , pp. 839-851
    • Papanikou, E.1    Karamanou, S.2    Economou, A.3
  • 27
    • 0031559943 scopus 로고    scopus 로고
    • In vitro virus: Bonding of mRNA bearing puromycin at the 3'-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro
    • Nemoto N, Miyamoto-Sato E, Husimi Y, Yanagawa H (1997) In vitro virus: Bonding of mRNA bearing puromycin at the 3'-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro. FEBS Lett 414(2): 405-408.
    • (1997) FEBS Lett , vol.414 , Issue.2 , pp. 405-408
    • Nemoto, N.1    Miyamoto-Sato, E.2    Husimi, Y.3    Yanagawa, H.4
  • 28
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins
    • Roberts RW, Szostak JW (1997) RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc Natl Acad Sci USA 94(23): 12297-12302.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.23 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 29
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes J, Plückthun A (1997) In vitro selection and evolution of functional proteins by using ribosome display. Proc Natl Acad Sci USA 94(10): 4937-4942.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.10 , pp. 4937-4942
    • Hanes, J.1    Plückthun, A.2
  • 30
    • 1542297763 scopus 로고    scopus 로고
    • CIS display: In vitro selection of peptides from libraries of protein-DNA complexes
    • Odegrip R, et al. (2004) CIS display: In vitro selection of peptides from libraries of protein-DNA complexes. Proc Natl Acad Sci USA 101(9): 2806-2810.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.9 , pp. 2806-2810
    • Odegrip, R.1
  • 32
    • 55749110716 scopus 로고    scopus 로고
    • Production of membrane proteins using cellfree expression systems
    • Schwarz D, Dötsch V, Bernhard F (2008) Production of membrane proteins using cellfree expression systems. Proteomics 8(19): 3933-3946.
    • (2008) Proteomics , vol.8 , Issue.19 , pp. 3933-3946
    • Schwarz, D.1    Dötsch, V.2    Bernhard, F.3
  • 33
    • 39149133696 scopus 로고    scopus 로고
    • Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases
    • Xie K, Dalbey RE (2008) Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases. Nat Rev Microbiol 6(3): 234-244.
    • (2008) Nat Rev Microbiol , vol.6 , Issue.3 , pp. 234-244
    • Xie, K.1    Dalbey, R.E.2
  • 34
    • 23244445172 scopus 로고    scopus 로고
    • Development of a minimal cell-free translation system for the synthesis of presecretory and integral membrane proteins
    • Kuruma Y, Nishiyama K, Shimizu Y, Müller M, Ueda T (2005) Development of a minimal cell-free translation system for the synthesis of presecretory and integral membrane proteins. Biotechnol Prog 21(4): 1243-1251.
    • (2005) Biotechnol Prog , vol.21 , Issue.4 , pp. 1243-1251
    • Kuruma, Y.1    Nishiyama, K.2    Shimizu, Y.3    Müller, M.4    Ueda, T.5
  • 35
    • 43049142194 scopus 로고    scopus 로고
    • High yield cell-free production of integral membrane proteins without refolding or detergents
    • Wuu JJ, Swartz JR (2008) High yield cell-free production of integral membrane proteins without refolding or detergents. Biochim Biophys Acta 1778(5): 1237-1250.
    • (2008) Biochim Biophys Acta , vol.1778 , Issue.5 , pp. 1237-1250
    • Wuu, J.J.1    Swartz, J.R.2
  • 36
    • 84859175970 scopus 로고    scopus 로고
    • Automated forward and reverse ratcheting of DNA in a nanopore at 5-Å precision
    • Cherf GM, et al. (2012) Automated forward and reverse ratcheting of DNA in a nanopore at 5-Å precision. Nat Biotechnol 30(4): 344-348.
    • (2012) Nat Biotechnol , vol.30 , Issue.4 , pp. 344-348
    • Cherf, G.M.1
  • 37
    • 0030465241 scopus 로고    scopus 로고
    • Characterization of individual polynucleotide molecules using a membrane channel
    • Kasianowicz JJ, Brandin E, Branton D, Deamer DW (1996) Characterization of individual polynucleotide molecules using a membrane channel. Proc Natl Acad Sci USA 93(24): 13770-13773.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.24 , pp. 13770-13773
    • Kasianowicz, J.J.1    Brandin, E.2    Branton, D.3    Deamer, D.W.4
  • 38
    • 0041843734 scopus 로고    scopus 로고
    • Partitioning of individual flexible polymers into a nanoscopic protein pore
    • Movileanu L, Cheley S, Bayley H (2003) Partitioning of individual flexible polymers into a nanoscopic protein pore. Biophys J 85(2): 897-910.
    • (2003) Biophys J , vol.85 , Issue.2 , pp. 897-910
    • Movileanu, L.1    Cheley, S.2    Bayley, H.3
  • 40
    • 0032762996 scopus 로고    scopus 로고
    • Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid, and polyuridylic acid as homopolymers or as segments within single RNA molecules
    • Akeson M, Branton D, Kasianowicz JJ, Brandin E, Deamer DW (1999) Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid, and polyuridylic acid as homopolymers or as segments within single RNA molecules. Biophys J 77(6): 3227-3233.
    • (1999) Biophys J , vol.77 , Issue.6 , pp. 3227-3233
    • Akeson, M.1    Branton, D.2    Kasianowicz, J.J.3    Brandin, E.4    Deamer, D.W.5
  • 41
    • 69249146604 scopus 로고    scopus 로고
    • Quantifying epistatic interactions among the components constituting the protein translation system
    • Matsuura T, Kazuta Y, Aita T, Adachi J, Yomo T (2009) Quantifying epistatic interactions among the components constituting the protein translation system. Mol Syst Biol 5: 297.
    • (2009) Mol Syst Biol , vol.5 , pp. 297
    • Matsuura, T.1    Kazuta, Y.2    Aita, T.3    Adachi, J.4    Yomo, T.5
  • 42
    • 11144220854 scopus 로고    scopus 로고
    • A vesicle bioreactor as a step toward an artificial cell assembly
    • Noireaux V, Libchaber A (2004) A vesicle bioreactor as a step toward an artificial cell assembly. Proc Natl Acad Sci USA 101(51): 17669-17674.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.51 , pp. 17669-17674
    • Noireaux, V.1    Libchaber, A.2
  • 43
    • 0038061507 scopus 로고    scopus 로고
    • Production of unilamellar vesicles Using an inverted emulsion
    • Pautot S, Frisken BJ, Weitz DA (2003) Production of unilamellar vesicles Using an inverted emulsion. Langmuir 19(7): 2870-2879.
    • (2003) Langmuir , vol.19 , Issue.7 , pp. 2870-2879
    • Pautot, S.1    Frisken, B.J.2    Weitz, D.A.3
  • 44
    • 79959344274 scopus 로고    scopus 로고
    • Kinetic analysis of β-galactosidase and β-glucuronidase tetramerization coupled with protein translation
    • Matsuura T, Hosoda K, Ichihashi N, Kazuta Y, Yomo T (2011) Kinetic analysis of β-galactosidase and β-glucuronidase tetramerization coupled with protein translation. J Biol Chem 286(25): 22028-22034.
    • (2011) J Biol Chem , vol.286 , Issue.25 , pp. 22028-22034
    • Matsuura, T.1    Hosoda, K.2    Ichihashi, N.3    Kazuta, Y.4    Yomo, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.