메뉴 건너뛰기




Volumn 2, Issue 3, 2007, Pages 715-726

Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; PROTEIN SUBUNIT; MULTIPROTEIN COMPLEX;

EID: 34347228701     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2007.73     Document Type: Article
Times cited : (558)

References (39)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R. & Mann, M. Mass spectrometry-based proteomics. Nature 422, 198-207 (2003).
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 2
    • 0028926048 scopus 로고
    • Protein-protein interactions:mEthods for detection and analysis
    • Phizicky, E.M. & Fields, S. Protein-protein interactions:mEthods for detection and analysis. Am. Soc. Microbiol. 59, 94-123 (1995).
    • (1995) Am. Soc. Microbiol , vol.59 , pp. 94-123
    • Phizicky, E.M.1    Fields, S.2
  • 3
    • 0000217562 scopus 로고
    • Electrospray and Taylor-Cone theory, Dole's beam of macromolecules at last?
    • Wilm, M.S. & Mann, M. Electrospray and Taylor-Cone theory, Dole's beam of macromolecules at last? Int. J. Mass Spectrom. Ion Process 136, 167 (1994).
    • (1994) Int. J. Mass Spectrom. Ion Process , vol.136 , pp. 167
    • Wilm, M.S.1    Mann, M.2
  • 4
    • 0037086063 scopus 로고    scopus 로고
    • Tandem Mass Spectrometer for Improved Transmission and Analysis of Large Macromolecular Assemblies
    • Sobott, F., Hernandez, H., McCammon, M.G., Tito, M.A. & Robinson, C.V. A Tandem Mass Spectrometer for Improved Transmission and Analysis of Large Macromolecular Assemblies. Anal. Chem. 74, 1402-1407 (2002).
    • (2002) Anal. Chem , vol.74 , pp. 1402-1407
    • Sobott, F.1    Hernandez, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.A.5
  • 6
    • 33749240797 scopus 로고    scopus 로고
    • Probing genuine strong interactions and post-translational modifications in the heterogeneous yeast exosome protein complex
    • Synowsky, S.A., van den Heuvel, R.H., Mohammed, S., Pijnappel, P.W. & Heck, A.J. Probing genuine strong interactions and post-translational modifications in the heterogeneous yeast exosome protein complex. Mol. Cell. Proteomics 5, 1581-1592 (2006).
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1581-1592
    • Synowsky, S.A.1    van den Heuvel, R.H.2    Mohammed, S.3    Pijnappel, P.W.4    Heck, A.J.5
  • 7
    • 33747347236 scopus 로고    scopus 로고
    • Structural organization of the 19S proteasome lid: Insights from MS of intact complexes
    • Sharon, M., Taverner, T., Ambroggio, X.I., Deshaies, R.J. & Robinson, C.V. Structural organization of the 19S proteasome lid: Insights from MS of intact complexes. PloS Biol. 4, 1314-1323 (2006).
    • (2006) PloS Biol , vol.4 , pp. 1314-1323
    • Sharon, M.1    Taverner, T.2    Ambroggio, X.I.3    Deshaies, R.J.4    Robinson, C.V.5
  • 8
    • 20444427617 scopus 로고    scopus 로고
    • Heptameric (L12)(6)/L10 rather than canonical pentameric complexes are found by tandem MS of intact ribosomes from thermophilic bacteria
    • Ilag, L.L. et al. Heptameric (L12)(6)/L10 rather than canonical pentameric complexes are found by tandem MS of intact ribosomes from thermophilic bacteria. Proc. Natl. Acad. Sci. USA 102, 8192-8197 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8192-8197
    • Ilag, L.L.1
  • 9
    • 0036712695 scopus 로고    scopus 로고
    • Oligomeric structure of proclavaminic acid amidino hydrolase: Evolution of a hydrolytic enzyme in clavulanic acid biosynthesis
    • Elkins, J.M. et al. Oligomeric structure of proclavaminic acid amidino hydrolase: Evolution of a hydrolytic enzyme in clavulanic acid biosynthesis. Biochem. J. 366, 423-434 (2002).
    • (2002) Biochem. J , vol.366 , pp. 423-434
    • Elkins, J.M.1
  • 10
    • 0037064096 scopus 로고    scopus 로고
    • Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry
    • Sobott, F., Benesch, J.L., Vierling, E. & Robinson, C.V. Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry. J. Biol. Chem. 277, 38921-38929 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 38921-38929
    • Sobott, F.1    Benesch, J.L.2    Vierling, E.3    Robinson, C.V.4
  • 11
    • 29244481662 scopus 로고    scopus 로고
    • L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers
    • Keetch, C.A. et al. L55P transthyretin accelerates subunit exchange and leads to rapid formation of hybrid tetramers. J. Biol. Chem. 280, 41667-41674 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 41667-41674
    • Keetch, C.A.1
  • 12
    • 33745195658 scopus 로고    scopus 로고
    • Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism
    • Remaut, H. et al. Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism. Mol. Cell. 22, 831-842 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 831-842
    • Remaut, H.1
  • 13
    • 0029794153 scopus 로고    scopus 로고
    • Probing the nature of non-covalent interactions by mass spectrometry. A study of protein-CoA ligand binding and assembly
    • Robinson, C.V. et al. Probing the nature of non-covalent interactions by mass spectrometry. A study of protein-CoA ligand binding and assembly. J. Am. Chem. Soc. 118, 8646-8653 (1996).
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 8646-8653
    • Robinson, C.V.1
  • 14
    • 0030621966 scopus 로고    scopus 로고
    • Studying noncovalent protein complexes by electrospray ionization mass spectrometry
    • Loo, J.A. Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom. Rev. 16, 1-23 (1997).
    • (1997) Mass Spectrom. Rev , vol.16 , pp. 1-23
    • Loo, J.A.1
  • 15
    • 0002124332 scopus 로고    scopus 로고
    • Electrospray ionization of large multiply charged species proceeds via Dolés charged residue mechanism
    • Fernandez de la Mora, J. Electrospray ionization of large multiply charged species proceeds via Dolés charged residue mechanism. Anal. Chim. Acta 406, 93-104 (2000).
    • (2000) Anal. Chim. Acta , vol.406 , pp. 93-104
    • Fernandez de la Mora, J.1
  • 16
    • 1542723081 scopus 로고    scopus 로고
    • Collisional cooling of large ions in electrospray mass spectrometry
    • Chemushevich, I.V. & Thomson, B.A. Collisional cooling of large ions in electrospray mass spectrometry. Anal. Chem. 76, 1754-1760 (2004).
    • (2004) Anal. Chem , vol.76 , pp. 1754-1760
    • Chemushevich, I.V.1    Thomson, B.A.2
  • 17
    • 0033583731 scopus 로고    scopus 로고
    • Detection of the intact GroEL chaperonin assembly by mass spectrometry
    • Rostom, A.A. & Robinson, C.V. Detection of the intact GroEL chaperonin assembly by mass spectrometry. J. Am. Chem. Soc. 121 4718-4719 (1999).
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 4718-4719
    • Rostom, A.A.1    Robinson, C.V.2
  • 18
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin, A.C. et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415, 141-147 (2002).
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1
  • 19
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho, Y. et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415 180-183 (2002).
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1
  • 20
    • 33644555054 scopus 로고    scopus 로고
    • Proteome survey reveals modularity of the yeast cell machinery
    • Gavin, A.C. et al. Proteome survey reveals modularity of the yeast cell machinery. Nature 440, 631-636 (2006).
    • (2006) Nature , vol.440 , pp. 631-636
    • Gavin, A.C.1
  • 21
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut, G. et al. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17, 1030-1032 (1999).
    • (1999) Nat. Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1
  • 22
    • 23044506580 scopus 로고    scopus 로고
    • Ion-ion and ion-molecule reactions at the surface of proteins produced by nanospray. Information on the number of acidic residues and control of the number of ionized acidic and basic residues
    • Verkerk, U.H. & Kebarle, P. Ion-ion and ion-molecule reactions at the surface of proteins produced by nanospray. Information on the number of acidic residues and control of the number of ionized acidic and basic residues. J. Am. Soc. Mass Spectrom. 16, 1325-1341 (2005).
    • (2005) J. Am. Soc. Mass Spectrom , vol.16 , pp. 1325-1341
    • Verkerk, U.H.1    Kebarle, P.2
  • 23
    • 3242671533 scopus 로고    scopus 로고
    • Buffer loading for counteracting metal salt-induced signal suppression in electrospray ionization
    • Iavarone, A.T., Udekwu, O.A. & Williams, E.R. Buffer loading for counteracting metal salt-induced signal suppression in electrospray ionization. Anal. Chem. 76, 3944-3950 (2004).
    • (2004) Anal. Chem , vol.76 , pp. 3944-3950
    • Iavarone, A.T.1    Udekwu, O.A.2    Williams, E.R.3
  • 24
    • 0036135966 scopus 로고    scopus 로고
    • Use of lectrospray ionization mass spectrometry to study binding interactions between a replication terminator protein and DNA
    • Kapur, A., Beck, J.L., Brown, S.E., Dixon, N.E. & Sheil, M.M. Use of lectrospray ionization mass spectrometry to study binding interactions between a replication terminator protein and DNA. Protein Sci. 11, 147-157 (2002).
    • (2002) Protein Sci , vol.11 , pp. 147-157
    • Kapur, A.1    Beck, J.L.2    Brown, S.E.3    Dixon, N.E.4    Sheil, M.M.5
  • 25
    • 0035894046 scopus 로고    scopus 로고
    • Influence of pressure in the first pumping stage on analyte desolvation and fragmentation in nano-ESI MS
    • Schmidt, A., Bahr, U. & Karas, M. Influence of pressure in the first pumping stage on analyte desolvation and fragmentation in nano-ESI MS. Anal. Chem. 73, 6040-6046 (2001).
    • (2001) Anal. Chem , vol.73 , pp. 6040-6046
    • Schmidt, A.1    Bahr, U.2    Karas, M.3
  • 26
    • 44049116161 scopus 로고
    • Collisional focusing effects in radiofrequency quadrupoles
    • Douglas, D.J. & French, J.B. Collisional focusing effects in radiofrequency quadrupoles. J. Am. Soc. Mass Spectrom. 3, 398-408 (1992).
    • (1992) J. Am. Soc. Mass Spectrom , vol.3 , pp. 398-408
    • Douglas, D.J.1    French, J.B.2
  • 27
    • 0028447420 scopus 로고    scopus 로고
    • Light-Wahl, K.J., Schwartz, B.L. & Smith, R.D. Observation of the noncovalent quaternary associations of proteins by electrospray ionization mass spectrometry. J. Am. Chem. Soc. 116, 5271-5278 (1994).
    • Light-Wahl, K.J., Schwartz, B.L. & Smith, R.D. Observation of the noncovalent quaternary associations of proteins by electrospray ionization mass spectrometry. J. Am. Chem. Soc. 116, 5271-5278 (1994).
  • 28
    • 4344666177 scopus 로고    scopus 로고
    • Characterising electrosprayed biomolecules using tandem-MS-the noncovalent GroEL chaperonin assembly
    • Sobott, F. & Robinson, C.V. Characterising electrosprayed biomolecules using tandem-MS-the noncovalent GroEL chaperonin assembly. Int. J. Mass. Spectrom. 236, 25-32 (2004).
    • (2004) Int. J. Mass. Spectrom , vol.236 , pp. 25-32
    • Sobott, F.1    Robinson, C.V.2
  • 30
    • 0002884477 scopus 로고    scopus 로고
    • Changes in bulk solution pH caused by the inherent controlled-current electrolytic process of an electrospray ion source
    • Van Berkel, G.J., Zhou, F. & Aronson, J.T. Changes in bulk solution pH caused by the inherent controlled-current electrolytic process of an electrospray ion source. Int. J. Mass Spectrom. Ion Process 162 55-68 (1997).
    • (1997) Int. J. Mass Spectrom. Ion Process , vol.162 , pp. 55-68
    • Van Berkel, G.J.1    Zhou, F.2    Aronson, J.T.3
  • 32
    • 0036237693 scopus 로고    scopus 로고
    • ORF6 from the clavulanic acid gene cluster of Streptomyces clavuligerus has ornithine acetyltransferase activity
    • Kershaw, N.J. et al. ORF6 from the clavulanic acid gene cluster of Streptomyces clavuligerus has ornithine acetyltransferase activity. Eur. J. Biochem. 269, 2052-2059 (2002).
    • (2002) Eur. J. Biochem , vol.269 , pp. 2052-2059
    • Kershaw, N.J.1
  • 33
    • 7244239509 scopus 로고    scopus 로고
    • Application of electrospray ionization mass spectrometry to study the hydrophobic interaction between the epsilon and theta subunits of DNA polymerase III
    • Gupta, R., Hamdan, S.M., Dixon, N.E., Sheil, M.M. & Beck, J.L. Application of electrospray ionization mass spectrometry to study the hydrophobic interaction between the epsilon and theta subunits of DNA polymerase III. Protein Sci. 13, 2878-2887 (2004).
    • (2004) Protein Sci , vol.13 , pp. 2878-2887
    • Gupta, R.1    Hamdan, S.M.2    Dixon, N.E.3    Sheil, M.M.4    Beck, J.L.5
  • 34
    • 33745192792 scopus 로고    scopus 로고
    • Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies
    • Benesch, J.L., Aquilina, J.A., Ruotolo, B.T., Sobott, F. & Robinson, C.V. Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies. Chem. Biol. 13, 597-605 (2006).
    • (2006) Chem. Biol , vol.13 , pp. 597-605
    • Benesch, J.L.1    Aquilina, J.A.2    Ruotolo, B.T.3    Sobott, F.4    Robinson, C.V.5
  • 35
    • 0037420384 scopus 로고    scopus 로고
    • Origin of asymmetric charge partitioning in the dissociation of gas-phase protein homodimers
    • Jurchen, J.C. & Williams, E.R. Origin of asymmetric charge partitioning in the dissociation of gas-phase protein homodimers. J. Am. Chem. Soc. 125, 2817-2826 (2003).
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 2817-2826
    • Jurchen, J.C.1    Williams, E.R.2
  • 36
    • 0034639980 scopus 로고    scopus 로고
    • Electrospray time-offlight mass spectrometry of the intact MS2 virus capsid
    • Tito, M.A., Tars, K., Valegard, K., Hajdu, J. & Robinson, C.V. Electrospray time-offlight mass spectrometry of the intact MS2 virus capsid. J. Am. Chem. Soc. 122, 3550-3551 (2000).
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 3550-3551
    • Tito, M.A.1    Tars, K.2    Valegard, K.3    Hajdu, J.4    Robinson, C.V.5
  • 37
    • 33748368713 scopus 로고    scopus 로고
    • Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes
    • McKay, A.R., Ruotolo, B.T., Ilag, L.L. & Robinson, C.V. Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes. J. Am. Chem. Soc. 128, 11433-11442 (2006).
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 11433-11442
    • McKay, A.R.1    Ruotolo, B.T.2    Ilag, L.L.3    Robinson, C.V.4
  • 38
    • 33747475197 scopus 로고    scopus 로고
    • Resolving stoichiometries and oligomeric states of glutamate synthase protein complexes with curve fitting and simulation of electrospray mass spectra
    • van Breukelen, B., Barendregt, A., Heck, A.J. & van den Heuvel, R.H. Resolving stoichiometries and oligomeric states of glutamate synthase protein complexes with curve fitting and simulation of electrospray mass spectra. Rap. Comm. Mass Spectrom. 20, 2490-2496 (2006).
    • (2006) Rap. Comm. Mass Spectrom , vol.20 , pp. 2490-2496
    • van Breukelen, B.1    Barendregt, A.2    Heck, A.J.3    van den Heuvel, R.H.4
  • 39
    • 0033524941 scopus 로고    scopus 로고
    • Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs
    • Kambach, C. et al. Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. Cell 96, 375-387 (1999).
    • (1999) Cell , vol.96 , pp. 375-387
    • Kambach, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.