A secreted fungal histidine- and alanine-rich protein regulates metal ion homeostasis and oxidative stress

© 2020 The Authors. New Phytologist © 2020 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 227(2020), 4 vom: 15. Aug., Seite 1174-1188
1. Verfasser: Nostadt, Robin (VerfasserIn)
Weitere Verfasser: Hilbert, Magdalena, Nizam, Shadab, Rovenich, Hanna, Wawra, Stephan, Martin, Jörg, Küpper, Hendrik, Mijovilovich, Ana, Ursinus, Astrid, Langen, Gregor, Hartmann, Marcus D, Lupas, Andrei N, Zuccaro, Alga
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2020
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Bipolaris sorokiniana Blumeria graminis Prussian blue staining cell wall appositions effector iron reactive oxygen species (ROS) µXRF mehr... Histidine 4QD397987E Alanine OF5P57N2ZX
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100 1 |a Nostadt, Robin  |e verfasserin  |4 aut 
245 1 2 |a A secreted fungal histidine- and alanine-rich protein regulates metal ion homeostasis and oxidative stress 
264 1 |c 2020 
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500 |a Date Completed 14.05.2021 
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500 |a Citation Status MEDLINE 
520 |a © 2020 The Authors. New Phytologist © 2020 New Phytologist Trust. 
520 |a Like pathogens, beneficial endophytic fungi secrete effector proteins to promote plant colonization, for example, through perturbation of host immunity. The genome of the root endophyte Serendipita indica encodes a novel family of highly similar, small alanine- and histidine-rich proteins, whose functions remain unknown. Members of this protein family carry an N-terminal signal peptide and a conserved C-terminal DELD motif. Here we report on the functional characterization of the plant-responsive DELD family protein Dld1 using a combination of structural, biochemical, biophysical and cytological analyses. The crystal structure of Dld1 shows an unusual, monomeric histidine zipper consisting of two antiparallel coiled-coil helices. Similar to other histidine-rich proteins, Dld1 displays varying affinity to different transition metal ions and undergoes metal ion- and pH-dependent unfolding. Transient expression of mCherry-tagged Dld1 in barley leaf and root tissue suggests that Dld1 localizes to the plant cell wall and accumulates at cell wall appositions during fungal penetration. Moreover, recombinant Dld1 enhances barley root colonization by S. indica, and inhibits H2 O2 -mediated radical polymerization of 3,3'-diaminobenzidine. Our data suggest that Dld1 has the potential to enhance micronutrient accessibility for the fungus and to interfere with oxidative stress and reactive oxygen species homeostasis to facilitate host colonization 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Bipolaris sorokiniana 
650 4 |a Blumeria graminis 
650 4 |a Prussian blue staining 
650 4 |a cell wall appositions 
650 4 |a effector 
650 4 |a iron 
650 4 |a reactive oxygen species (ROS) 
650 4 |a µXRF 
650 7 |a Histidine  |2 NLM 
650 7 |a 4QD397987E  |2 NLM 
650 7 |a Alanine  |2 NLM 
650 7 |a OF5P57N2ZX  |2 NLM 
700 1 |a Hilbert, Magdalena  |e verfasserin  |4 aut 
700 1 |a Nizam, Shadab  |e verfasserin  |4 aut 
700 1 |a Rovenich, Hanna  |e verfasserin  |4 aut 
700 1 |a Wawra, Stephan  |e verfasserin  |4 aut 
700 1 |a Martin, Jörg  |e verfasserin  |4 aut 
700 1 |a Küpper, Hendrik  |e verfasserin  |4 aut 
700 1 |a Mijovilovich, Ana  |e verfasserin  |4 aut 
700 1 |a Ursinus, Astrid  |e verfasserin  |4 aut 
700 1 |a Langen, Gregor  |e verfasserin  |4 aut 
700 1 |a Hartmann, Marcus D  |e verfasserin  |4 aut 
700 1 |a Lupas, Andrei N  |e verfasserin  |4 aut 
700 1 |a Zuccaro, Alga  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t The New phytologist  |d 1979  |g 227(2020), 4 vom: 15. Aug., Seite 1174-1188  |w (DE-627)NLM09818248X  |x 1469-8137  |7 nnns 
773 1 8 |g volume:227  |g year:2020  |g number:4  |g day:15  |g month:08  |g pages:1174-1188 
856 4 0 |u http://dx.doi.org/10.1111/nph.16606  |3 Volltext 
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