Structural highlights
Publication Abstract from PubMed
Few secreted proteins involved in plant infection common to necrotrophic bacteria, fungi and oomycetes have been identified except for plant cell wall-degrading enzymes. Here we study a family of iron-binding proteins that is present in Gram-negative and Gram-positive bacteria, fungi, oomycetes and some animals. Homolog proteins in the phytopathogenic bacterium Dickeya dadantii (IbpS) and the fungal necrotroph Botrytis cinerea (BcIbp) are involved in plant infection. IbpS is secreted, can bind iron and copper, and protects the bacteria against H2O2-induced death. Its 1.7 A crystal structure reveals a classical Venus Fly trap fold that forms dimers in solution and in the crystal. We propose that secreted Ibp proteins binds exogenous metals and thus limit intracellular metal accumulation and ROS formation in the microorganisms.
A secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species.,Liu L, Gueguen-Chaignon V, Goncalves IR, Rascle C, Rigault M, Dellagi A, Loisel E, Poussereau N, Rodrigue A, Terradot L, Condemine G Nat Commun. 2019 Oct 24;10(1):4853. doi: 10.1038/s41467-019-12826-x. PMID:31649262[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu L, Gueguen-Chaignon V, Goncalves IR, Rascle C, Rigault M, Dellagi A, Loisel E, Poussereau N, Rodrigue A, Terradot L, Condemine G. A secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species. Nat Commun. 2019 Oct 24;10(1):4853. doi: 10.1038/s41467-019-12826-x. PMID:31649262 doi:http://dx.doi.org/10.1038/s41467-019-12826-x
