Watching protein structure at work in living cells using NMR spectroscopy

Current Opinion in Chemical Biology

Volumn 16, Issue 5-6, 2012, Pages 609-613

  Tochio, Hidehito ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

FLUORINE; NITROGEN 15;

BACTERIAL CELL; CELL STRAIN 293F; CELL STRAIN COS7; ESCHERICHIA COLI; FLUORINE NUCLEAR MAGNETIC RESONANCE; HELA CELL; HUMAN; MAMMAL CELL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OOCYTE; PICHIA PASTORIS; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; XENOPUS LAEVIS;

ANIMALS; HUMANS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN INTERACTION MAPPING; PROTEINS;

BACTERIA (MICROORGANISMS); MAMMALIA;

EID: 84872267371     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2012.10.022     Document Type: Review

References (33)

1. Manley S., Gunzenhäuser J., Olivier N. A starter kit for point-localization super-resolution imaging. Curr Opin Chem Biol 2011, 15:813-821. (Internet).
2. de Graaf R.A. In vivo NMR Spectroscopy: Principles and Techniques 2008, Wiley-Interscience.
3. Serber Z., Selenko P., Hänsel R., Reckel S., Löhr F., Ferrell J.E., Wagner G., Dötsch V. Investigating macromolecules inside cultured and injected cells by in-cell NMR spectroscopy. Nat Protoc 2006, 1:2701-2709. (Internet).
4. Serber Z., Keatinge-Clay A.T., Ledwidge R., Kelly A.E., Miller S.M., Dötsch V. High-resolution macromolecular NMR spectroscopy inside living cells. J Am Chem Soc 2001, 123:2446-2447. (Internet).
5. Selenko P., Serber Z., Gadea B., Ruderman J., Wagner G. Quantitative NMR analysis of the protein G B1 domain in Xenopus laevis egg extracts and intact oocytes. Proc Natl Acad Sci U S A 2006, 103:11904-11909. (Internet).
6. Sakai T., Tochio H., Tenno T., Ito Y., Kokubo T., Hiroaki H., Shirakawa M. In-cell NMR spectroscopy of proteins inside Xenopus laevis oocytes. J Biomol NMR 2006, 36:179-188. (Internet).
7. Inomata K., Ohno A., Tochio H., Isogai S., Tenno T., Nakase I., Takeuchi T., Futaki S., Ito Y., Hiroaki H., et al. High-resolution multi-dimensional NMR spectroscopy of proteins in human cells. Nature 2009, 458:106-109. (Internet).
8. Ogino S., Kubo S., Umemoto R., Huang S., Nishida N., Shimada I. Observation of NMR signals from proteins introduced into living mammalian cells by reversible membrane permeabilization using a pore-forming toxin, streptolysin O. J Am Chem Soc 2009, 131:10834-10835. (Internet).
9. Robinson K.E., Reardon P.N., Spicer L.D. Protein NMR Techniques 2012, Springer, New York, (Internet).
10. Arnesano F., Banci L., Bertini I., Felli I.C., Losacco M., Natile G. Probing the interaction of cisplatin with the human copper chaperone Atox1 by solution and in-cell NMR spectroscopy. J Am Chem Soc 2011, 133:18361-18369. (Internet).
11. Burz D.S., Dutta K., Cowburn D., Shekhtman A. In-cell NMR for protein-protein interactions (STINT-NMR). Nat Protoc 2006, 1:146-152. (Internet).
12. Banci L., Barbieri L., Bertini I., Cantini F., Luchinat E. In-cell NMR in E. coli to monitor maturation steps of hSOD1. PLoS ONE 2011, 6:e23561. (Internet).
13. Sakakibara D., Sasaki A., Ikeya T., Hamatsu J., Hanashima T., Mishima M., Yoshimasu M., Hayashi N., Mikawa T., Wälchli M., et al. Protein structure determination in living cells by in-cell NMR spectroscopy. Nature 2009, 458:102-105. (Internet).
14. Ikeya T., Sasaki A., Sakakibara D., Shigemitsu Y., Hamatsu J., Hanashima T., Mishima M., Yoshimasu M., Hayashi N., Mikawa T., et al. NMR protein structure determination in living E. coli cells using nonlinear sampling. Nat Protoc 2010, 5:1051-1060. (Internet).
15. Lippens G., Landrieu I., Hanoulle X. Studying posttranslational modifications by in-cell NMR. Chem Biol 2008, 15:311-312. (Internet).
16. Selenko P., Frueh D.P., Elsaesser S.J., Haas W., Gygi S.P., Wagner G. In situ observation of protein phosphorylation by high-resolution NMR spectroscopy. Nat Struct Mol Biol 2008, 15:321-329. (Internet).
17. Bodart J.F., Wieruszeski J.M., Amniai L., Leroy A., Landrieu I., Rousseau-Lescuyer A., Vilain J.P., Lippens G. NMR observation of Tau in Xenopus oocytes. J Magn Reson 2008, (Internet).
18. Hänsel R., Foldynová-Trantírková S., Löhr F., Buck J., Bongartz E., Bamberg E., Schwalbe H., Dötsch V., Trantírek L. Evaluation of parameters critical for observing nucleic acids inside living Xenopus laevis oocytes by in-cell NMR spectroscopy. J Am Chem Soc 2009, 131:15761-15768. (Internet).
19. Nakase I., Takeuchi T., Tanaka G., Futaki S. Methodological and cellular aspects that govern the internalization mechanisms of arginine-rich cell-penetrating peptides. Adv Drug Deliv Rev 2008, 60:598-607. (Internet).
20. Nakase I., Akita H., Kogure K., Gräslund A., Langel U., Harashima H., Futaki S. Efficient intracellular delivery of nucleic acid pharmaceuticals using cell-penetrating peptides. Acc Chem Res 2011, XXX. (Internet).
21. Takeuchi T., Kosuge M., Tadokoro A., Sugiura Y., Nishi M., Kawata M., Sakai N., Matile S., Futaki S. Direct and rapid cytosolic delivery using cell-penetrating peptides mediated by pyrenebutyrate. ACS Chem Biol 2006, 1:299-303. (Internet).
22. Zhou H.-X., Rivas G., Minton A.P. Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences. Annu Rev Biophys 2008, 37:375-397. (Internet).
23. Elcock A.H. Models of macromolecular crowding effects and the need for quantitative comparisons with experiment. Curr Opin Struct Biol 2010, 20:196-206. (Internet).
24. Barnes C.O., Monteith W.B., Pielak G.J. Internal and global protein motion assessed with a fusion construct and in-cell NMR spectroscopy. Chembiochem: Eur J Chem Biol 2011, 12:390-391. (Internet).
25. Li C., Charlton L.M., Lakkavaram A., Seagle C., Wang G., Young G.B., Macdonald J.M., Pielak G.J. Differential dynamical effects of macromolecular crowding on an intrinsically disordered protein and a globular protein: implications for in-cell NMR spectroscopy. J Am Chem Soc 2008, 130:6310-6311. (Internet).
26. Schlesinger A.P., Wang Y., Tadeo X., Millet O., Pielak G.J. Macromolecular crowding fails to fold a globular protein in cells. J Am Chem Soc 2011, 133:8082-8085. (Internet).
27. Ignatova Z., Krishnan B., Bombardier J.P., Marcelino A.M.C., Hong J., Gierasch L.M. From the test tube to the cell: exploring the folding and aggregation of a beta-clam protein. Biopolymers 2007, 88:157-163. (Internet).
28. Luheshi L.M., Dobson C.M. Bridging the gap: from protein misfolding to protein misfolding diseases. FEBS Lett 2009, 583:2581-2586. (Internet).
29. Wang Q., Zhuravleva A., Gierasch L.M. Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy. Biochemistry 2011, 50:9225-9236. (Internet).
30. Crowley P.B., Chow E., Papkovskaia T. Protein interactions in the Escherichia coli cytosol: an impediment to in-cell NMR spectroscopy. Chembiochem: Eur J Chem Biol 2011, 12:1043-1048. (Internet).
31. Bertrand K., Reverdatto S., Burz D.S., Zitomer R., Shekhtman A. Structure of proteins in eukaryotic compartments. J Am Chem Soc 2012, 134:12798-12806. (Internet).
32. Xie J., Thapa R., Reverdatto S., Burz D.S., Shekhtman A. Screening of small molecule interactor library by using in-cell NMR spectroscopy (SMILI-NMR). J Med Chem 2009, 52:3516-3522. (Internet).
33. Li C., Wang G.-F., Wang Y., Creager-Allen R., Lutz E.A., Scronce H., Slade K.M., Ruf R.A.S., Mehl R.A., Pielak G.J. Protein (19)F NMR in Escherichia coli. J Am Chem Soc 2010, 132:321-327. (Internet).