메뉴 건너뛰기




Volumn 11, Issue 2, 2012, Pages 1454-1459

Nanodiscs and SILAC-based mass spectrometry to identify a membrane protein interactome

Author keywords

MalFGK2; membrane proteome; nanodiscs; protein lipid interactions; SecYEG; SILAC; YidC

Indexed keywords

BACTERIAL PROTEIN; CELL EXTRACT; INTEGRASE; INTEGRASE YIDC; MALTOSE BINDING PROTEIN; MALTOSE TRANSPORTER MALFGK2; MEMBRANE PROTEIN; NANODISC; PERIPLASMIC PROTEIN; PROTEIN MALE; PROTEIN SECA; PROTEIN SYD; UNCLASSIFIED DRUG;

EID: 84863037366     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr200846y     Document Type: Article
Times cited : (24)

References (36)
  • 1
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin, E.; Heijne, G. V. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms Protein Sci. 1998, 7 (4) 1029-1038
    • (1998) Protein Sci. , vol.7 , Issue.4 , pp. 1029-1038
    • Wallin, E.1    Heijne, G.V.2
  • 2
    • 50049135906 scopus 로고    scopus 로고
    • Proteome of the Escherichia coli envelope and technological challenges in membrane proteome analysis
    • Weiner, J. H.; Li, L. Proteome of the Escherichia coli envelope and technological challenges in membrane proteome analysis Biochim. Biophys. Acta 2008, 1778 (9) 1698-1713
    • (2008) Biochim. Biophys. Acta , vol.1778 , Issue.9 , pp. 1698-1713
    • Weiner, J.H.1    Li, L.2
  • 3
    • 48849107198 scopus 로고    scopus 로고
    • Solubilization of membrane protein complexes for blue native PAGE
    • Reisinger, V.; Eichacker, L. A. Solubilization of membrane protein complexes for blue native PAGE J. Proteomics 2008, 71 (3) 277-283
    • (2008) J. Proteomics , vol.71 , Issue.3 , pp. 277-283
    • Reisinger, V.1    Eichacker, L.A.2
  • 4
    • 34848889247 scopus 로고    scopus 로고
    • Methods for mapping of interaction networks involving membrane proteins
    • Hooker, B. S.; Bigelow, D. J.; Lin, C. T. Methods for mapping of interaction networks involving membrane proteins Biochem. Biophys. Res. Commun. 2007, 363 (3) 457-461
    • (2007) Biochem. Biophys. Res. Commun. , vol.363 , Issue.3 , pp. 457-461
    • Hooker, B.S.1    Bigelow, D.J.2    Lin, C.T.3
  • 5
    • 70349327690 scopus 로고    scopus 로고
    • Exploring the inner membrane proteome of Escherichia coli: Which proteins are eluding detection and why?
    • Bernsel, A.; Daley, D. O. Exploring the inner membrane proteome of Escherichia coli: Which proteins are eluding detection and why? Trends Microbiol. 2009, 17 (10) 444-449
    • (2009) Trends Microbiol. , vol.17 , Issue.10 , pp. 444-449
    • Bernsel, A.1    Daley, D.O.2
  • 6
    • 57549088143 scopus 로고    scopus 로고
    • Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome
    • Diaz-Mejia, J. J.; Babu, M.; Emili, A. Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome FEMS Microbiol. Rev. 2009, 33 (1) 66-97
    • (2009) FEMS Microbiol. Rev. , vol.33 , Issue.1 , pp. 66-97
    • Diaz-Mejia, J.J.1    Babu, M.2    Emili, A.3
  • 7
    • 55749112976 scopus 로고    scopus 로고
    • Membrane proteins and membrane proteomics
    • Tan, S.; Tan, H. T.; Chung, M. C. M. Membrane proteins and membrane proteomics PROTEOMICS 2008, 8 (19) 3924-3932
    • (2008) PROTEOMICS , vol.8 , Issue.19 , pp. 3924-3932
    • Tan, S.1    Tan, H.T.2    Chung, M.C.M.3
  • 8
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into Nanodiscs
    • Bayburt, T. H.; Sligar, S. G. Membrane protein assembly into Nanodiscs FEBS Lett. 2010, 584 (9) 1721-1727
    • (2010) FEBS Lett. , vol.584 , Issue.9 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 9
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S.-E.; Blagoev, B.; Kratchmarova, I.; Kristensen, D. B.; Steen, H.; Pandey, A.; Mann, M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics Mol. Cell. Proteomics 2002, 1 (5) 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , Issue.5 , pp. 376-386
    • Ong, S.-E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 11
    • 77954733211 scopus 로고    scopus 로고
    • Reconstitution of the SecY translocon in nanodiscs
    • Dalal, K.; Duong, F. Reconstitution of the SecY translocon in nanodiscs Methods Mol. Biol. 2010, 619, 145-156
    • (2010) Methods Mol. Biol. , vol.619 , pp. 145-156
    • Dalal, K.1    Duong, F.2
  • 12
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster, L. J.; de Hoog, C. L.; Mann, M. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors Proc. Natl. Acad. Sci. U. S. A. 2003, 100 (10) 5813-5818
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , Issue.10 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 13
    • 43849108709 scopus 로고    scopus 로고
    • Identification of cognate host targets and specific ubiquitylation sites on the Salmonella SPI-1 effector SopB/SigD
    • Rogers, L. D.; Kristensen, A. R.; Boyle, E. C.; Robinson, D. P.; Ly, R. T.; Finlay, B. B.; Foster, L. J. Identification of cognate host targets and specific ubiquitylation sites on the Salmonella SPI-1 effector SopB/SigD J. Proteomics 2008, 71 (1) 97-108
    • (2008) J. Proteomics , vol.71 , Issue.1 , pp. 97-108
    • Rogers, L.D.1    Kristensen, A.R.2    Boyle, E.C.3    Robinson, D.P.4    Ly, R.T.5    Finlay, B.B.6    Foster, L.J.7
  • 15
    • 80052163308 scopus 로고    scopus 로고
    • The SecY complex: Conducting the orchestra of protein translocation
    • Dalal, K.; Duong, F. The SecY complex: Conducting the orchestra of protein translocation Trends Cell Biol. 2011, 9, 506-514
    • (2011) Trends Cell Biol. , vol.9 , pp. 506-514
    • Dalal, K.1    Duong, F.2
  • 18
    • 0026344236 scopus 로고
    • SecA protein needs both acidic phospholipids and SecY/E protein for functional high-affinity binding to the Escherichia coli plasma membrane
    • Hendrick, J. P.; Wickner, W. SecA protein needs both acidic phospholipids and SecY/E protein for functional high-affinity binding to the Escherichia coli plasma membrane J. Biol. Chem. 1991, 266 (36) 24596-24600
    • (1991) J. Biol. Chem. , vol.266 , Issue.36 , pp. 24596-24600
    • Hendrick, J.P.1    Wickner, W.2
  • 19
    • 0025019705 scopus 로고
    • The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
    • Lill, R.; Dowhan, W.; Wickner, W. The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins Cell 1990, 60 (2) 271-280
    • (1990) Cell , vol.60 , Issue.2 , pp. 271-280
    • Lill, R.1    Dowhan, W.2    Wickner, W.3
  • 20
    • 34248583785 scopus 로고    scopus 로고
    • Generation of ribosome nascent chain complexes for structural and functional studies
    • Schaffitzel, C.; Ban, N. Generation of ribosome nascent chain complexes for structural and functional studies J. Struct. Biol. 2007, 158 (3) 463-471
    • (2007) J. Struct. Biol. , vol.158 , Issue.3 , pp. 463-471
    • Schaffitzel, C.1    Ban, N.2
  • 21
    • 79953737877 scopus 로고    scopus 로고
    • The bacterial SRP receptor, SecA and the ribosome use overlapping binding sites on the SecY translocon
    • Kuhn, P.; Weiche, B.; Sturm, L.; Sommer, E.; Drepper, F.; Warscheid, B.; Sourjik, V.; Koch, H.-G. The bacterial SRP receptor, SecA and the ribosome use overlapping binding sites on the SecY translocon Traffic 2011, 12 (5) 563-578
    • (2011) Traffic , vol.12 , Issue.5 , pp. 563-578
    • Kuhn, P.1    Weiche, B.2    Sturm, L.3    Sommer, E.4    Drepper, F.5    Warscheid, B.6    Sourjik, V.7    Koch, H.-G.8
  • 22
    • 0034460877 scopus 로고    scopus 로고
    • Vanadate-induced trapping of nucleotides by purified maltose transport complex requires ATP hydrolysis
    • Sharma, S.; Davidson, A. L. Vanadate-induced trapping of nucleotides by purified maltose transport complex requires ATP hydrolysis J. Bacteriol. 2000, 182 (23) 6570-6576
    • (2000) J. Bacteriol. , vol.182 , Issue.23 , pp. 6570-6576
    • Sharma, S.1    Davidson, A.L.2
  • 23
    • 0019902462 scopus 로고
    • Role of the catabolite activator protein in the maltose regulon of Escherichia coli
    • Chapon, C. Role of the catabolite activator protein in the maltose regulon of Escherichia coli J. Bacteriol. 1982, 150 (2) 722-729
    • (1982) J. Bacteriol. , vol.150 , Issue.2 , pp. 722-729
    • Chapon, C.1
  • 24
    • 0028932110 scopus 로고
    • Differential expression of mal genes under cAMP and endogenous inducer control in nutrient-stressed Escherichia coli
    • Notley, L.; Ferenci, T. Differential expression of mal genes under cAMP and endogenous inducer control in nutrient-stressed Escherichia coli Mol. Microbiol. 1995, 16 (1) 121-129
    • (1995) Mol. Microbiol. , vol.16 , Issue.1 , pp. 121-129
    • Notley, L.1    Ferenci, T.2
  • 25
    • 0025687504 scopus 로고
    • Regulation of the maltose transport system of Escherichia coli by the glucose-specific enzyme III of the phosphoenolpyruvate-sugar phosphotransferase system
    • Dean, D. A.; Reizer, J.; Nikaido, H.; Saier, M. H. Regulation of the maltose transport system of Escherichia coli by the glucose-specific enzyme III of the phosphoenolpyruvate-sugar phosphotransferase system J. Biol. Chem. 1990, 265 (34) 21005-21010
    • (1990) J. Biol. Chem. , vol.265 , Issue.34 , pp. 21005-21010
    • Dean, D.A.1    Reizer, J.2    Nikaido, H.3    Saier, M.H.4
  • 26
    • 0031768746 scopus 로고    scopus 로고
    • The ATP-binding cassette subunit of the maltose transporter MalK antagonizes MalT, the activator of the Escherichia coli mal regulon
    • Panagiotidis, C. H.; Boos, W.; Shuman, H. A. The ATP-binding cassette subunit of the maltose transporter MalK antagonizes MalT, the activator of the Escherichia coli mal regulon Mol. Microbiol. 1998, 30 (3) 535-546
    • (1998) Mol. Microbiol. , vol.30 , Issue.3 , pp. 535-546
    • Panagiotidis, C.H.1    Boos, W.2    Shuman, H.A.3
  • 27
    • 0032515148 scopus 로고    scopus 로고
    • Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli
    • Sääf, A.; Monné, M.; de Gier, J.-W.; von Heijne, G. Membrane topology of the 60-kDa Oxa1p homologue from Escherichia coli J. Biol. Chem. 1998, 273 (46) 30415-30418
    • (1998) J. Biol. Chem. , vol.273 , Issue.46 , pp. 30415-30418
    • Sääf, A.1    Monné, M.2    De Gier, J.-W.3    Von Heijne, G.4
  • 28
    • 41949094573 scopus 로고    scopus 로고
    • Crystal structure of the major periplasmic domain of the bacterial membrane protein assembly facilitator YidC
    • Oliver, D. C.; Paetzel, M. Crystal structure of the major periplasmic domain of the bacterial membrane protein assembly facilitator YidC J. Biol. Chem. 2008, 283 (8) 5208-5216
    • (2008) J. Biol. Chem. , vol.283 , Issue.8 , pp. 5208-5216
    • Oliver, D.C.1    Paetzel, M.2
  • 29
    • 44049107026 scopus 로고    scopus 로고
    • The crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleft
    • Ravaud, S.; Stjepanovic, G.; Wild, K.; Sinning, I. The crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleft J. Biol. Chem. 2008, 283 (14) 9350-9358
    • (2008) J. Biol. Chem. , vol.283 , Issue.14 , pp. 9350-9358
    • Ravaud, S.1    Stjepanovic, G.2    Wild, K.3    Sinning, I.4
  • 30
    • 42049104126 scopus 로고    scopus 로고
    • Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role for these proteins in quality control upon insertion of bacterial inner membrane proteins
    • van Bloois, E.; Dekker, H. L.; Fröderberg, L.; Houben, E. N. G.; Urbanus, M. L.; de Koster, C. G.; de Gier, J.-W.; Luirink, J. Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role for these proteins in quality control upon insertion of bacterial inner membrane proteins FEBS Lett. 2008, 582 (10) 1419-1424
    • (2008) FEBS Lett. , vol.582 , Issue.10 , pp. 1419-1424
    • Van Bloois, E.1    Dekker, H.L.2    Fröderberg, L.3    Houben, E.N.G.4    Urbanus, M.L.5    De Koster, C.G.6    De Gier, J.-W.7    Luirink, J.8
  • 31
    • 55749083826 scopus 로고    scopus 로고
    • Fully denaturing two-dimensional electrophoresis of membrane proteins: A critical update
    • Rabilloud, T.; Chevallet, M.; Luche, S.; Lelong, C. Fully denaturing two-dimensional electrophoresis of membrane proteins: A critical update Proteomics 2008, 8 (19) 3965-3973
    • (2008) Proteomics , vol.8 , Issue.19 , pp. 3965-3973
    • Rabilloud, T.1    Chevallet, M.2    Luche, S.3    Lelong, C.4
  • 32
    • 79959456892 scopus 로고    scopus 로고
    • Advances in the mass spectrometry of membrane proteins: From individual proteins to intact complexes
    • Barrera, N. P.; Robinson, C. V. Advances in the mass spectrometry of membrane proteins: From individual proteins to intact complexes Annu. Rev. Biochem. 2011, 80 (1) 247-271
    • (2011) Annu. Rev. Biochem. , vol.80 , Issue.1 , pp. 247-271
    • Barrera, N.P.1    Robinson, C.V.2
  • 33
    • 34548854237 scopus 로고    scopus 로고
    • Proteins at membrane surfaces-a review of approaches
    • Macher, B. A.; Yen, T.-Y. Proteins at membrane surfaces-a review of approaches Mol. BioSyst. 2007, 3 (10) 705-713
    • (2007) Mol. BioSyst. , vol.3 , Issue.10 , pp. 705-713
    • MacHer, B.A.1    Yen, T.-Y.2
  • 34
    • 34247214427 scopus 로고    scopus 로고
    • Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA
    • Alami, M.; Dalal, K.; Lelj-Garolla, B.; Sligar, S. G.; Duong, F. Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA EMBO J. 2007, 26 (8) 1995-2004
    • (2007) EMBO J. , vol.26 , Issue.8 , pp. 1995-2004
    • Alami, M.1    Dalal, K.2    Lelj-Garolla, B.3    Sligar, S.G.4    Duong, F.5
  • 36
    • 0034426807 scopus 로고    scopus 로고
    • Site-specific photocrosslinking to probe interactions of Arf1 with proteins involved in budding of COPI vesicles
    • Fischer, K. D.; Helms, J. B.; Zhao, L.; Wieland, F. T. Site-specific photocrosslinking to probe interactions of Arf1 with proteins involved in budding of COPI vesicles Methods 2000, 20 (4) 455-464
    • (2000) Methods , vol.20 , Issue.4 , pp. 455-464
    • Fischer, K.D.1    Helms, J.B.2    Zhao, L.3    Wieland, F.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.