Advertisement

Biomolecular NMR Assignments

, Volume 7, Issue 1, pp 109–112 | Cite as

Backbone and sidechain 1H, 13C and 15N chemical shift assignments of the hydrophobin MPG1 from the rice blast fungus Magnaporthe oryzae

  • Anthony A. Rey
  • Antoine Hocher
  • Ann H. Kwan
  • Margaret SundeEmail author
Article

Abstract

Fungal hydrophobins are secreted proteins that self-assemble at hydrophobic:hydrophilic interfaces. They are essential for a variety of processes in the fungal life cycle, including mediating interactions with surfaces and infection of hosts. The fungus Magnaporthe oryzae, the causative agent of rice blast, relies on the unique properties of hydrophobins to infect cultivated rice as well as over 50 different grass species. The hydrophobin MPG1 is highly expressed during rice blast pathogenesis and has been implicated during host infection. Here we report the backbone and sidechain assignments for the class I hydrophobin MPG1 from the rice blast fungus Magnaporthe oryzae.

Keywords

Rice blast disease MPG1 Hydrophobin Functional amyloid NMR assignment 

Notes

Acknowledgments

This work was supported by an Australian Research Council Discovery Project (DP0879121). MS was supported by a NHMRC RD Wright Career Development Fellowship.

Conflict of interest

The authors declare that they have no conflict of interest.

References

  1. Cai M, Huang Y, Sakaguchi K, Clore GM, Gronenborn AM, Craigie R (1998) An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli. J Biomol NMR 11:97–102CrossRefGoogle Scholar
  2. Catanzariti AM, Soboleva TA, Jans DA, Board PG, Baker RT (2004) An efficient system for high-level expression and easy purification of authentic recombinant proteins. Protein Sci 13:1331–1339CrossRefGoogle Scholar
  3. Goddard TD, Kneller DG. SPARKY. University of California at San Francisco. http://www.cgl.ucsf.edu/home/sparky/
  4. Kwan AH, Winefield RD, Sunde M, Matthews JM, Haverkamp RG, Templeton MD, Mackay JP (2006) Structural basis for rodlet assembly in fungal hydrophobins. Proc Natl Acad Sci USA 103:3621–3626ADSCrossRefGoogle Scholar
  5. Mackay JP, Matthews JM, Winefield RD, Mackay LG, Haverkamp RG, Templeton MD (2001) The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures. Structure 9:83–91CrossRefGoogle Scholar
  6. Petersen TN, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8:785–786CrossRefGoogle Scholar
  7. Scholtmeijer K, Janssen MI, van Leeuwen MB, van Kooten TG, Hektor H, Wosten HA (2004) The use of hydrophobins to functionalize surfaces. Biomed Mater Eng 14:447–454Google Scholar
  8. Sharma D, Rajarathnam K (2000) 13C NMR chemical shifts can predict disulfide bond formation. J Biomol NMR 18:165–171CrossRefGoogle Scholar
  9. Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44:213–223CrossRefGoogle Scholar
  10. Skamnioti P, Gurr SJ (2009) Against the grain: safeguarding rice from rice blast disease. Trends Biotechnol 27:141–150CrossRefGoogle Scholar
  11. Sunde M, Kwan AH, Templeton MD, Beever RE, Mackay JP (2008) Structural analysis of hydrophobins. Micron 39:773–784CrossRefGoogle Scholar
  12. Talbot NJ, Kershaw MJ, Wakley GE, deVries OMH, Wessels JGH, Hamer JE (1996) MPG1 encodes a fungal hydrophobin involved in surface interactions during infection-related development of Magnaporthe grisea. Plant Cell 8:985–999Google Scholar
  13. Wang X, Permentier HP, Rink R, Kruijtzer JAW, Liskamp RMJ, Wosten HAB, Poolman B, Robillard GT (2004) Probing the self-assembly and the accompanying structural changes of hydrophobin SC3 on a hydrophobic surface by mass spectrometry. Biophys J 87:1919–1928CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2012

Authors and Affiliations

  • Anthony A. Rey
    • 1
  • Antoine Hocher
    • 1
  • Ann H. Kwan
    • 1
  • Margaret Sunde
    • 1
    • 2
    Email author
  1. 1.School of Molecular BioscienceUniversity of SydneySydneyAustralia
  2. 2.Discipline of PharmacologyUniversity of SydneySydneyAustralia

Personalised recommendations