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

Anthony A Rey; Antoine Hocher; Ann H Kwan; Margaret Sunde

doi:10.1007/s12104-012-9394-x

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

Biomol NMR Assign. 2013 Apr;7(1):109-12. doi: 10.1007/s12104-012-9394-x. Epub 2012 May 19.

Authors

Anthony A Rey¹, Antoine Hocher, Ann H Kwan, Margaret Sunde

Affiliation

¹ School of Molecular Bioscience, University of Sydney, Sydney, NSW, 2006, Australia.

PMID: 22610311
DOI: 10.1007/s12104-012-9394-x

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Fungal Proteins / chemistry*
Magnaporthe*
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular*
Solutions

Substances

Fungal Proteins
Solutions