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

被引:10
作者
Rey, Anthony A. [1 ]
Hocher, Antoine [1 ]
Kwan, Ann H. [1 ]
Sunde, Margaret [1 ]
机构
[1] Univ Sydney, Sch Mol Biosci, Sydney, NSW 2006, Australia
基金
澳大利亚国家健康与医学研究理事会; 澳大利亚研究理事会;
关键词
Rice blast disease; MPG1; Hydrophobin; Functional amyloid; NMR assignment; EFFICIENT; SURFACE;
D O I
10.1007/s12104-012-9394-x
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
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.
引用
收藏
页码:109 / 112
页数:4
相关论文
共 13 条
[1]   An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli [J].
Cai, ML ;
Huang, Y ;
Sakaguchi, K ;
Clore, GM ;
Gronenborn, AM ;
Craigie, R .
JOURNAL OF BIOMOLECULAR NMR, 1998, 11 (01) :97-102
[2]   An efficient system for high-level expression and easy purification of authentic recombinant proteins [J].
Catanzariti, AM ;
Soboleva, TA ;
Jans, DA ;
Board, PG ;
Baker, RT .
PROTEIN SCIENCE, 2004, 13 (05) :1331-1339
[3]  
Goddard T.D., SPARKY
[4]   Structural basis for rodlet assembly in fungal hydrophobins [J].
Kwan, AHY ;
Winefield, RD ;
Sunde, M ;
Matthews, JM ;
Haverkamp, RG ;
Templeton, MD ;
Mackay, JP .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (10) :3621-3626
[5]   The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures [J].
Mackay, JP ;
Matthews, JM ;
Winefield, RD ;
Mackay, LG ;
Haverkamp, RG ;
Templeton, MD .
STRUCTURE, 2001, 9 (02) :83-91
[6]   SignalP 4.0: discriminating signal peptides from transmembrane regions [J].
Petersen, Thomas Nordahl ;
Brunak, Soren ;
von Heijne, Gunnar ;
Nielsen, Henrik .
NATURE METHODS, 2011, 8 (10) :785-786
[7]  
Scholtmeijer K, 2004, BIO-MED MATER ENG, V14, P447
[8]   13C NMR chemical shifts can predict disulfide bond formation [J].
Sharma, D ;
Rajarathnam, K .
JOURNAL OF BIOMOLECULAR NMR, 2000, 18 (02) :165-171
[9]   TALOS plus : a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts [J].
Shen, Yang ;
Delaglio, Frank ;
Cornilescu, Gabriel ;
Bax, Ad .
JOURNAL OF BIOMOLECULAR NMR, 2009, 44 (04) :213-223
[10]   Against the grain: safeguarding rice from rice blast disease [J].
Skamnioti, Pari ;
Gurr, Sarah J. .
TRENDS IN BIOTECHNOLOGY, 2009, 27 (03) :141-150