Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry
10.1038/nmeth753
Crossref journal-article
Springer Science and Business Media LLC
Nature Methods (297)
Bibliography

van Duijn, E., Bakkes, P. J., Heeren, R. M. A., van den Heuvel, R. H. H., van Heerikhuizen, H., van der Vies, S. M., & Heck, A. J. R. (2005). Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry. Nature Methods, 2(5), 371–376.

Authors 7
  1. Esther van Duijn (first)
  2. Patrick J Bakkes (additional)
  3. Ron M A Heeren (additional)
  4. Robert H H van den Heuvel (additional)
  5. Harm van Heerikhuizen (additional)
  6. Saskia M van der Vies (additional)
  7. Albert J R Heck (additional)
References 38 Referenced 92
  1. Houry, W.A., Frishman, D., Eckerskorn, C., Lottspeich, F. & Hartl, F.U. Identification of in vivo substrates of the chaperonin GroEL. Nature 402, 147–154 (1999). (10.1038/45977) / Nature by WA Houry (1999)
  2. Hartl, F.U. & Hayer-Hartl, M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852–1858 (2002). (10.1126/science.1068408) / Science by FU Hartl (2002)
  3. Ellis, R.J. Molecular chaperones: inside and outside the Anfinsen cage. Curr. Biol. 11, R1038–R1040 (2001). (10.1016/S0960-9822(01)00620-0) / Curr. Biol. by RJ Ellis (2001)
  4. Sigler, P.B. et al. Structure and function in GroEL-mediated protein folding. Annu. Rev. Biochem. 67, 581–608 (1998). (10.1146/annurev.biochem.67.1.581) / Annu. Rev. Biochem. by PB Sigler (1998)
  5. Walters, C., Errington, N., Rowe, A.J. & Harding, S.E. Hydrolysable ATP is a requirement for the correct interaction of molecular chaperonins cpn60 and cpn10. Biochem. J. 364, 849–855 (2002). (10.1042/bj20011643) / Biochem. J. by C Walters (2002)
  6. van der Vies, S.M., Viitanen, P.V., Gatenby, A.A., Lorimer, G.H. & Jaenicke, R. Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60. Biochemistry 31, 3635–3644 (1992). (10.1021/bi00129a012) / Biochemistry by SM van der Vies (1992)
  7. Hunt, J.F., van der Vies, S.M., Henry, L. & Deisenhofer, J. Structural adaptations in the specialized bacteriophage T4 cochaperonin Gp31 expand the size of the Anfinsen cage. Cell 90, 361–371 (1997). (10.1016/S0092-8674(00)80343-8) / Cell by JF Hunt (1997)
  8. Langer, T., Pfeifer, G., Martin, J., Baumeister, W. & Hartl, F.U. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO J. 11, 4757–4765 (1992). (10.1002/j.1460-2075.1992.tb05581.x) / EMBO J. by T Langer (1992)
  9. Braig, K., Simon, M., Furuya, F., Hainfeld, J.F. & Horwich, A.L. A polypeptide bound by the chaperonin GroEL is localized within a central cavity. Proc. Natl. Acad. Sci. USA 90, 3978–3982 (1993). (10.1073/pnas.90.9.3978) / Proc. Natl. Acad. Sci. USA by K Braig (1993)
  10. Chen, S. et al. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature 371, 261–264 (1994). (10.1038/371261a0) / Nature by S Chen (1994)
  11. Braig, K. et al. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature 371, 578–586 (1994). (10.1038/371578a0) / Nature by K Braig (1994)
  12. Fiaux, J., Bertelsen, E.B., Horwich, A.L. & Wuthrich, K. NMR analysis of a 900K GroEL GroES complex. Nature 418, 207–211 (2002). (10.1038/nature00860) / Nature by J Fiaux (2002)
  13. Riek, R., Fiaux, J., Bertelsen, E.B., Horwich, A.L. & Wuthrich, K. Solution NMR techniques for large molecular and supramolecular structures. J. Am. Chem. Soc. 124, 12144–12153 (2002). (10.1021/ja026763z) / J. Am. Chem. Soc. by R Riek (2002)
  14. Griswold, I.J. & Dahlquist, F.W. Bigger is better: megadalton protein NMR in solution. Nat. Struct. Biol. 9, 567–568 (2002). (10.1038/nsb0802-567) / Nat. Struct. Biol. by IJ Griswold (2002)
  15. van den Heuvel, R.H. & Heck, A.J. Native protein mass spectrometry: from intact oligomers to functional machineries. Curr. Opin. Chem. Biol. 8, 519–526 (2004). (10.1016/j.cbpa.2004.08.006) / Curr. Opin. Chem. Biol. by RH van den Heuvel (2004)
  16. Verentchikov, A.N., Ens, W. & Standing, K.G. Reflecting time-of-flight mass spectrometer with an electrospray ion source and orthogonal extraction. Anal. Chem. 66, 126–133 (1994). (10.1021/ac00073a022) / Anal. Chem. by AN Verentchikov (1994)
  17. Loo, J.A. Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom. Rev. 16, 1–23 (1997). (10.1002/(SICI)1098-2787(1997)16:1<1::AID-MAS1>3.0.CO;2-L) / Mass Spectrom. Rev. by JA Loo (1997)
  18. Heck, A.J. & Van Den Heuvel, R.H. Investigation of intact protein complexes by mass spectrometry. Mass Spectrom. Rev. 23, 368–389 (2004). (10.1002/mas.10081) / Mass Spectrom. Rev. by AJ Heck (2004)
  19. Robinson, C.V. Protein complexes take flight. Nat. Struct. Biol. 9, 505–506 (2002). (10.1038/nsb0702-505) / Nat. Struct. Biol. by CV Robinson (2002)
  20. Heuvel, R.H. & Heck, A.J. Native protein mass spectrometry: from intact oligomers to functional machineries. Curr. Opin. Chem. Biol. 8, 519–526 (2004). (10.1016/j.cbpa.2004.08.006) / Curr. Opin. Chem. Biol. by RH Heuvel (2004)
  21. Hernandez, H. & Robinson, C.V. Dynamic protein complexes: insights from mass spectrometry. J. Biol. Chem. 276, 46685–46688 (2001). (10.1074/jbc.R100024200) / J. Biol. Chem. by H Hernandez (2001)
  22. Robinson, C.V. et al. Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry. Nature 372, 646–651 (1994). (10.1038/372646a0) / Nature by CV Robinson (1994)
  23. Coyle, J.E., Jaeger, J., Gross, M., Robinson, C.V. & Radford, S.E. Structural and mechanistic consequences of polypeptide binding by GroEL. Fold. Des. 2, R93–104 (1997). (10.1016/S1359-0278(97)00046-1) / Fold. Des. by JE Coyle (1997)
  24. Coyle, J.E. et al. GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism. Nat. Struct. Biol. 6, 683–690 (1999). (10.1038/10735) / Nat. Struct. Biol. by JE Coyle (1999)
  25. Rostom, A.A. & Robinson, C.V. Detection of the intact GroEL chaperonin assembly by mass spectrometry. J. Am. Chem. Soc. 121, 4718–4719 (1999). (10.1021/ja990238r) / J. Am. Chem. Soc. by AA Rostom (1999)
  26. Krutchinsky, A.N., Chernushevich, I.V., Spicer, V.L., Ens, W. & Standing, K.G. Collisional damping interface for an electrospray ionization time-of-flight mass spectrometer. J. Am. Soc. Mass Spectrom. 9, 569–579 (1998). (10.1016/S1044-0305(98)00027-0) / J. Am. Soc. Mass Spectrom. by AN Krutchinsky (1998)
  27. 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). (10.1021/ac0110552) / Anal. Chem. by F Sobott (2002)
  28. Tahallah, N., Pinkse, M., Maier, C.S. & Heck, A.J. The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument. Rapid Commun. Mass Spectrom. 15, 596–601 (2001). (10.1002/rcm.275) / Rapid Commun. Mass Spectrom. by N Tahallah (2001)
  29. Chernushevich, I.V. & Thomson, B.A. Collisional cooling of large ions in electrospray mass spectrometry. Anal. Chem. 76, 1754–1760 (2004). (10.1021/ac035406j) / Anal. Chem. by IV Chernushevich (2004)
  30. Jackson, G.S. et al. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry 32, 2554–2563 (1993). (10.1021/bi00061a013) / Biochemistry by GS Jackson (1993)
  31. Burston, S.G., Ranson, N.A. & Clarke, A.R. The origins and consequences of asymmetry in the chaperonin reaction cycle. J. Mol. Biol. 249, 138–152 (1995). (10.1006/jmbi.1995.0285) / J. Mol. Biol. by SG Burston (1995)
  32. Laemmli, U.K., Beguin, F. & Gujer-Kellenberger, G. A factor preventing the major head protein of bacteriophage T4 from random aggregation. J. Mol. Biol. 47, 69–85 (1970). (10.1016/0022-2836(70)90402-X) / J. Mol. Biol. by UK Laemmli (1970)
  33. van der Vies, S.M., Gatenby, A.A. & Georgopoulos, C. Bacteriophage T4 encodes a cochaperonin that can substitute for Escherichia coli GroES in protein folding. Nature 368, 654–656 (1994). (10.1038/368654a0) / Nature by SM van der Vies (1994)
  34. Hartl, F.U. Molecular chaperones in cellular protein folding. Nature 381, 571–579 (1996). (10.1038/381571a0) / Nature by FU Hartl (1996)
  35. Bukau, B. & Horwich, A.L. The Hsp70 and Hsp60 chaperone machines. Cell 92, 351–366 (1998). (10.1016/S0092-8674(00)80928-9) / Cell by B Bukau (1998)
  36. Bakkes, P.J., Faber, B.W., van Heerikhuizen, H. & van der Vies, S.M. The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein. Proc. Natl. Acad. Sci. USA (in the press). (10.1073/pnas.0500048102)
  37. Xu, Z., Horwich, A.L. & Sigler, P.B. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388, 741–750 (1997). (10.1038/41944) / Nature by Z Xu (1997)
  38. Koonin, E.V. & van der Vies, S.M. Conserved sequence motifs in bacterial and bacteriophage chaperonins. Trends Biochem. Sci. 20, 14–15 (1995). (10.1016/S0968-0004(00)88941-0) / Trends Biochem. Sci. by EV Koonin (1995)
Dates
Type When
Created 20 years, 4 months ago (April 21, 2005, 3:32 p.m.)
Deposited 2 years, 3 months ago (May 18, 2023, 7:58 p.m.)
Indexed 1 year ago (Aug. 4, 2024, 7:34 p.m.)
Issued 20 years, 4 months ago (April 21, 2005)
Published 20 years, 4 months ago (April 21, 2005)
Published Online 20 years, 4 months ago (April 21, 2005)
Published Print 20 years, 3 months ago (May 1, 2005)
Funders 0

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@article{van_Duijn_2005, title={Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry}, volume={2}, ISSN={1548-7105}, url={http://dx.doi.org/10.1038/nmeth753}, DOI={10.1038/nmeth753}, number={5}, journal={Nature Methods}, publisher={Springer Science and Business Media LLC}, author={van Duijn, Esther and Bakkes, Patrick J and Heeren, Ron M A and van den Heuvel, Robert H H and van Heerikhuizen, Harm and van der Vies, Saskia M and Heck, Albert J R}, year={2005}, month=apr, pages={371–376} }