Protein complexes gain momentum

Current Opinion in Structural Biology

Volumn 12, Issue 6, 2002, Pages 729-734

  Sobott, Frank ^a   Robinson, Carol V ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; PROTEIN SUBUNIT;

BIOLOGICAL MONITORING; GENOME; MACROMOLECULE; MASS SPECTROMETRY; MOLECULAR BIOLOGY; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEOMICS; REVIEW; STOICHIOMETRY;

EID: 0036913741     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(02)00400-1     Document Type: Review

References (28)

1. Miranker A.D. Protein complexes and analysis of their assembly by mass spectrometry. Curr Opin Struct Biol. 10:2000;601-606.
2. Loo J.A. Electrospray ionisation mass spectrometry: a technology for studying noncovalent macromolecular complexes. Int J Mass Spectrom. 200:2000;175-186. A brief history of the development and application of gentle ionisation methods for the analysis of noncovalent complexes, with emphasis on ESI-MS of proteins. Experimental parameters are discussed and several examples of protein complexes are given.
3. Karas M., Bahr U., Dülcks T. Nano-electrospray ionisation mass spectrometry: addressing analytical problems beyond routine. Fresenius J Anal Chem. 366:2000;669-676.
4. Tahallah N., Pinkse M., Maier C.S., Heck A.J.R. The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionisation orthogonal time-of-flight instrument. Rapid Commun Mass Spectrom. 15:2001;596-601.
5. 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. 73:2001;6040-6046.
6. Sobott F., Hernández 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. 74:2002;1402-1407.
7. Rostom A.A., Fucini P., Benjamin D.R., Juenemann R., Nierhaus K.H., Hartl F.U., Dobson C.M., Robinson C.V. Detection and selective dissociation of intact ribosomes in the mass spectrometer. Proc Natl Acad Sci USA. 97:2000;5185-5190.
8. Van Berkel W.J.H., van den Heuvel R.H.H., Versluis C., Heck A.J.R. Detection of intact megaDalton protein assemblies of vanillyl-alcohol oxidase by mass spectrometry. Protein Sci. 9:2000;435-439.
9. Zal F., Chausson F., Leize E., van Dorsselaer A., Lallier F.H., Green B.N. Quadrupole time-of-flight MS of the native hemocyanin of the deep-sea crab bythograea thermydron. Biomacromolecules. 3:2002;229-231.
10. Standing K.G. Timing the flight of biomolecules: a personal perspective. Int J Mass Spectrom. 200:2000;597-610. A review of the development of TOF analysers over the past 50 years and their use in combination with different techniques for the gentle ionisation of biomolecules.
11. Mann M., Hendrickson R.C., Pandey A. Analysis of proteins and proteomes by mass spectrometry. Annu Rev Biochem. 70:2001;437-473. An introduction to sample preparation, ionisation techniques and instrumentation is followed by a comprehensive review of current proteomics methods.
12. Verma R., Chen S., Feldman R., Schieltz D., Yates J., Dohmen J., Deshaies R.J. Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol Biol Cell. 11:2000;3425-3439.
13. Gavin A.C., Bosche M., Krause R., Grandi P., Marzioch M., Bauer A., Schultz J., Rick J.M., Michon A.M., Cruciat C.M., et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature. 415:2002;141-147. A large-scale study of protein interactions in S. cerevisiae using tandem-affinity purification and MS. A total of 589 protein complexes have been purified and new cellular roles have been proposed for 344 proteins.
14. Ho Y., Gruhler A., Heilbut A., Bader G.D., Moore L., Adams S.L., Millar A., Taylor P., Bennett K., Boutilier K., et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature. 415:2002;180-183. In a similar approach to [13••], the identified complexes covered 25% of the yeast proteome and revealed many previously unknown protein interactions, for example, in signalling pathways and the DNA damage response.
15. Von Mering C., Krause R., Snel B., Cornell M., Oliver S.G., Fields S., Bork P. Comparative assessment of large-scale data sets of protein-protein interactions. Nature. 417:2002;399-403.
16. Rogniaux H., Sanglier S., Strupat K., Azza S., Roitel O., Ball V., Tritsch D., Branlant G., van Dorsselaer A. MS as a novel approach to probe cooperativity in multimeric enzymatic systems. Anal Biochem. 291:2001;48-61.
17. McCammon M.G., Scott D.J., Keetch C.A., Greene L.H., Purkey H.E., Petrassi H.M., Kelly J.W., Robinson C.V. Screening transthyretin amyloid fibril inhibitors: characterization of novel multiprotein, multiligand complexes by mass spectrometry. Structure. 10:2002;851-863. Nano-ESI TOF-MS has been used to detect transthyretin tetramers and their dissociative behaviour in the mass spectrometer, and to screen different ligands that potentially stabilise the tetrameric complex.
18. Tito M.A., Miller J., Walker N., Griffin K.F., Williamson E.D., Despeyroux-Hill D., Titball R.W., Robinson C.V. Probing molecular interactions in intact antibody: antigen complexes, an electrospray time-of-flight mass spectrometry approach. Biophys J. 81:2001;3503-3509.
19. Elkins J.M., Clifton I.J., Hernandez H., Robinson C.V., Schofield C.J., Hewitson K.S. Oligomeric structure of proclavaminate amidino hydrolase-anatomy of an enzyme catalyzing intermediate engineering during antibiotic biosynthesis. Biochem J. 366:2002;423-434.
20. Strupat K., Rogniaux H., van Dorsselaer A., Roth J., Vogl T. Calcium-induced noncovalently linked tetramers of MRP8 and MRP14 are confirmed by electrospray ionisation-mass analysis. J Am Soc Mass Spectrom. 11:2000;780-788.
21. Rappsilber J., Siniossoglou S., Hurt E.C., Mann M. A generic strategy to analyze the spatial organization of multi-protein complexes by cross-linking and mass spectrometry. Anal Chem. 72:2000;267-275. A generic approach to the structural investigation of protein complexes, combining gene tagging for the purification of protein complexes with chemical cross-linking and MS analysis of the digestion products.
22. Tito M.A., Miller J., Griffin K.F., Williamson E.D., Titball R.W., Robinson C.V. Macromolecular organization of the Yersinia pestis capsular F1 antigen: insights from time-of-flight mass spectrometry. Protein Sci. 10:2001;2408-2413.
23. Green B.N., Gotoh T., Suzuki T., Zal F., Lallier F.H., Toulmond A., Vinogradov S.N. Observation of large, non-covalent globin subassemblies in the approximately 3600 kDa hexagonal bilayer hemoglobins by electrospray ionisation time-of-flight mass spectrometry. J Mol Biol. 309:2001;553-560.
24. Fändrich M., Tito M.A., Leroux M.R., Rostom A.A., Hartl F.U., Dobson C.M., Robinson C.V. Observation of the non-covalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry. Proc Natl Acad Sci USA. 97:2000;14151-14155.
25. Sobott F., Benesch J.L.P., 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. 277:2002;38921-38929. The first kinetic study of the dynamic interactions in multimeric protein complexes by MS. Subunit exchange between dodecameric small HSPs was followed in real time and found to proceed predominantly via dimeric subunits.
26. Tito M.A., Tars K., Valegard K., Hajdu J., Robinson C.V. Electrospray time-of-flight MS of the intact MS2 virus capsid. J Am Chem Soc. 122:2000;3550-3551.
27. Bacher G., Szymanski W.W., Kaufman S.L., Zollner P., Blaas D., Allmaier G. Charge-reduced nano electrospray ionisation combined with differential mobility analysis of peptides, proteins, glycoproteins, noncovalent protein complexes and viruses. Mass J Spectrom. 36:2001;1038-1052. An introduction to the methods of DMA of ions is followed by an impressive range of examples, from peptides to noncovalent biocomplexes to intact viruses.
28. Fuerstenau S.D., Benner W.H., Thomas J.J., Brugidou C., Bothner B., Siuzdak G. MS of an intact virus. Angew Chem Int Ed. 40:2001;541-544. Charge-detectionMS, an evolving technique for the analysis of particles in the mega-Dalton range, is demonstrated on two viruses with molecular masses of 6.5 MDa and 40.5 MDa.