메뉴 건너뛰기




Volumn 588, Issue 20, 2014, Pages 3761-3769

MemStar: A one-shot Escherichia coli-based approach for high-level bacterial membrane protein production

Author keywords

Escherichia coli; High throughput; Membrane protein production; X ray crystallography

Indexed keywords

BACTERIAL PROTEIN; ISOPROPYL THIOGALACTOSIDE; MEMBRANE PROTEIN; PROTEIN NAPA; SODIUM PROTON EXCHANGE PROTEIN; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; OUTER MEMBRANE PROTEIN;

EID: 84907286117     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.08.025     Document Type: Article
Times cited : (26)

References (39)
  • 1
    • 84887403382 scopus 로고    scopus 로고
    • Structural basis for action by diverse antidepressants on biogenic amine transporters
    • H. Wang, A. Goehring, K.H. Wang, A. Penmatsa, R. Ressler, and E. Gouaux Structural basis for action by diverse antidepressants on biogenic amine transporters Nature 503 2013 141 145
    • (2013) Nature , vol.503 , pp. 141-145
    • Wang, H.1    Goehring, A.2    Wang, K.H.3    Penmatsa, A.4    Ressler, R.5    Gouaux, E.6
  • 4
    • 49449114407 scopus 로고    scopus 로고
    • Co-evolving stability and conformational homogeneity of the human adenosine A2a receptor
    • F. Magnani, Y. Shibata, M.J. Serrano-Vega, and C.G. Tate Co-evolving stability and conformational homogeneity of the human adenosine A2a receptor Proc. Natl. Acad. Sci. U.S.A. 105 2008 10744 10749
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 10744-10749
    • Magnani, F.1    Shibata, Y.2    Serrano-Vega, M.J.3    Tate, C.G.4
  • 5
    • 77953133721 scopus 로고    scopus 로고
    • Tricks of the trade used to accelerate high-resolution structure determination of membrane proteins
    • Y. Sonoda, A. Cameron, S. Newstead, H. Omote, Y. Moriyama, M. Kasahara, S. Iwata, and D. Drew Tricks of the trade used to accelerate high-resolution structure determination of membrane proteins FEBS Lett. 584 2010 2539 2547
    • (2010) FEBS Lett. , vol.584 , pp. 2539-2547
    • Sonoda, Y.1    Cameron, A.2    Newstead, S.3    Omote, H.4    Moriyama, Y.5    Kasahara, M.6    Iwata, S.7    Drew, D.8
  • 7
    • 33645454462 scopus 로고    scopus 로고
    • Optimization of membrane protein overexpression and purification using GFP fusions
    • D. Drew, M. Lerch, E. Kunji, D.J. Slotboom, and J.W. de Gier Optimization of membrane protein overexpression and purification using GFP fusions Nat. Methods 3 2006 303 313
    • (2006) Nat. Methods , vol.3 , pp. 303-313
    • Drew, D.1    Lerch, M.2    Kunji, E.3    Slotboom, D.J.4    De Gier, J.W.5
  • 8
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • F.W. Studier Protein production by auto-induction in high density shaking cultures Protein Expr. Purif. 41 2005 207 234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 9
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • B. Miroux, and J.E. Walker Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels J. Mol. Biol. 260 1996 289 298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 11
    • 0035955445 scopus 로고    scopus 로고
    • Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli
    • D.E. Drew, G. von Heijne, P. Nordlund, and J.W. de Gier Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli FEBS Lett. 507 2001 220 224
    • (2001) FEBS Lett. , vol.507 , pp. 220-224
    • Drew, D.E.1    Von Heijne, G.2    Nordlund, P.3    De Gier, J.W.4
  • 12
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • F.W. Studier, and B.A. Moffatt Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes J. Mol. Biol. 189 1986 113 130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 13
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • J. Abramson, I. Smirnova, V. Kasho, G. Verner, H. Kaback, and S. Iwata Structure and mechanism of the lactose permease of Escherichia coli Science 301 2003 610 615
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.5    Iwata, S.6
  • 14
    • 80054991427 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT
    • N.J. Hu, S. Iwata, A.D. Cameron, and D. Drew Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT Nature 478 2011 408 411
    • (2011) Nature , vol.478 , pp. 408-411
    • Hu, N.J.1    Iwata, S.2    Cameron, A.D.3    Drew, D.4
  • 15
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Y. Huang, M.J. Lemieux, J. Song, M. Auer, and D.N. Wang Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli Science 301 2003 616 620
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 17
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Y. Wang, Y. Zhang, and Y. Ha Crystal structure of a rhomboid family intramembrane protease Nature 444 2006 179 180
    • (2006) Nature , vol.444 , pp. 179-180
    • Wang, Y.1    Zhang, Y.2    Ha, Y.3
  • 19
    • 10344262632 scopus 로고    scopus 로고
    • The mechanism of ammonia transport based on the crystal structure of AmtB of Escherichia coli
    • L. Zheng, D. Kostrewa, S. Berneche, F.K. Winkler, and X.D. Li The mechanism of ammonia transport based on the crystal structure of AmtB of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 101 2004 17090 17095
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 17090-17095
    • Zheng, L.1    Kostrewa, D.2    Berneche, S.3    Winkler, F.K.4    Li, X.D.5
  • 20
    • 34648833810 scopus 로고    scopus 로고
    • Structure of the zinc transporter YiiP
    • M. Lu, and D. Fu Structure of the zinc transporter YiiP Science 317 2007 1746 1748
    • (2007) Science , vol.317 , pp. 1746-1748
    • Lu, M.1    Fu, D.2
  • 21
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • Y. Yin, X. He, P. Szewczyk, T. Nguyen, and G. Chang Structure of the multidrug transporter EmrD from Escherichia coli Science 312 2006 741 744
    • (2006) Science , vol.312 , pp. 741-744
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 26
    • 84883139208 scopus 로고    scopus 로고
    • Use of slow glucose feeding as supporting carbon source in lactose autoinduction medium improves the robustness of protein expression at different aeration conditions
    • K. Ukkonen, S. Mayer, A. Vasala, and P. Neubauer Use of slow glucose feeding as supporting carbon source in lactose autoinduction medium improves the robustness of protein expression at different aeration conditions Protein Expr. Purif. 91 2013 147 154
    • (2013) Protein Expr. Purif. , vol.91 , pp. 147-154
    • Ukkonen, K.1    Mayer, S.2    Vasala, A.3    Neubauer, P.4
  • 27
    • 33646011258 scopus 로고    scopus 로고
    • Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins
    • T. Kawate, and E. Gouaux Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins Structure 14 2006 673 681
    • (2006) Structure , vol.14 , pp. 673-681
    • Kawate, T.1    Gouaux, E.2
  • 29
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • D.O. Daley, M. Rapp, E. Granseth, K. Melen, D. Drew, and G. von Heijne Global topology analysis of the Escherichia coli inner membrane proteome Science 308 2005 1321 1323
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melen, K.4    Drew, D.5    Von Heijne, G.6
  • 30
    • 33646002978 scopus 로고    scopus 로고
    • Toxic protein expression in Escherichia coli using a rhamnose-based tightly regulated and tunable promoter system
    • M.J. Giacalone, A.M. Gentile, B.T. Lovitt, N.L. Berkley, C.W. Gunderson, and M.W. Surber Toxic protein expression in Escherichia coli using a rhamnose-based tightly regulated and tunable promoter system Biotechniques 40 2006 355 364
    • (2006) Biotechniques , vol.40 , pp. 355-364
    • Giacalone, M.J.1    Gentile, A.M.2    Lovitt, B.T.3    Berkley, N.L.4    Gunderson, C.W.5    Surber, M.W.6
  • 34
    • 84880703203 scopus 로고    scopus 로고
    • Improved production of membrane proteins in Escherichia coli by selective codon substitutions
    • M.H. Norholm, S. Toddo, M.T. Virkki, S. Light, G. von Heijne, and D.O. Daley Improved production of membrane proteins in Escherichia coli by selective codon substitutions FEBS Lett. 587 2013 2352 2358
    • (2013) FEBS Lett. , vol.587 , pp. 2352-2358
    • Norholm, M.H.1    Toddo, S.2    Virkki, M.T.3    Light, S.4    Von Heijne, G.5    Daley, D.O.6
  • 35
    • 58149478359 scopus 로고    scopus 로고
    • A green fluorescent protein screen for identification of well-expressed membrane proteins from a cohort of extremophilic organisms
    • J. Hammon, D.V. Palanivelu, J. Chen, C. Patel, and D.L. Minor Jr. A green fluorescent protein screen for identification of well-expressed membrane proteins from a cohort of extremophilic organisms Protein Sci. 18 2009 121 133
    • (2009) Protein Sci. , vol.18 , pp. 121-133
    • Hammon, J.1    Palanivelu, D.V.2    Chen, J.3    Patel, C.4    Minor, D.L.5
  • 36
    • 43149098999 scopus 로고    scopus 로고
    • GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae
    • D. Drew, S. Newstead, Y. Sonoda, H. Kim, G. von Heijne, and S. Iwata GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae Nat. Protoc. 3 2008 784 798
    • (2008) Nat. Protoc. , vol.3 , pp. 784-798
    • Drew, D.1    Newstead, S.2    Sonoda, Y.3    Kim, H.4    Von Heijne, G.5    Iwata, S.6
  • 38
    • 4344579363 scopus 로고    scopus 로고
    • A pedestrian guide to membrane protein crystallization
    • M.C. Wiener A pedestrian guide to membrane protein crystallization Methods 34 2004 364 372
    • (2004) Methods , vol.34 , pp. 364-372
    • Wiener, M.C.1
  • 39
    • 84855994087 scopus 로고    scopus 로고
    • Toward structure determination using membrane-protein nanocrystals and microcrystals
    • M.S. Hunter, and P. Fromme Toward structure determination using membrane-protein nanocrystals and microcrystals Methods 55 2011 387 404
    • (2011) Methods , vol.55 , pp. 387-404
    • Hunter, M.S.1    Fromme, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.