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

Autor: Nostadt R; Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Str. 10, 35043, Marburg, Germany., Hilbert M; Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Str. 10, 35043, Marburg, Germany., Nizam S; Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Str. 10, 35043, Marburg, Germany.; Cluster of Excellence on Plant Sciences (CEPLAS), Cologne Biocenter, Botanical Institute, University of Cologne, Zülpicher Str. 47b, 50674, Cologne, Germany., Rovenich H; Cluster of Excellence on Plant Sciences (CEPLAS), Cologne Biocenter, Botanical Institute, University of Cologne, Zülpicher Str. 47b, 50674, Cologne, Germany., Wawra S; Cluster of Excellence on Plant Sciences (CEPLAS), Cologne Biocenter, Botanical Institute, University of Cologne, Zülpicher Str. 47b, 50674, Cologne, Germany., Martin J; Max Planck Institute for Developmental Biology, Spemannstr. 35, 72076, Tübingen, Germany., Küpper H; Department of Plant Biophysics & Biochemistry, Biology Centre, Institute of Plant Molecular Biology, Czech Academy of Sciences, Branišovská 31/1160, 37005, České Budějovice, Czech Republic.; Department of Experimental Plant Biology, Faculty of Science, University of South Bohemia, Branišovská 31/1160, 37005, České Budějovice, Czech Republic., Mijovilovich A; Department of Plant Biophysics & Biochemistry, Biology Centre, Institute of Plant Molecular Biology, Czech Academy of Sciences, Branišovská 31/1160, 37005, České Budějovice, Czech Republic., Ursinus A; Max Planck Institute for Developmental Biology, Spemannstr. 35, 72076, Tübingen, Germany., Langen G; Cluster of Excellence on Plant Sciences (CEPLAS), Cologne Biocenter, Botanical Institute, University of Cologne, Zülpicher Str. 47b, 50674, Cologne, Germany., Hartmann MD; Max Planck Institute for Developmental Biology, Spemannstr. 35, 72076, Tübingen, Germany., Lupas AN; Max Planck Institute for Developmental Biology, Spemannstr. 35, 72076, Tübingen, Germany., Zuccaro A; Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Str. 10, 35043, Marburg, Germany.; Cluster of Excellence on Plant Sciences (CEPLAS), Cologne Biocenter, Botanical Institute, University of Cologne, Zülpicher Str. 47b, 50674, Cologne, Germany.
Jazyk: angličtina
Zdroj: The New phytologist [New Phytol] 2020 Aug; Vol. 227 (4), pp. 1174-1188. Date of Electronic Publication: 2020 May 16.
DOI: 10.1111/nph.16606
Abstrakt: 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 H 2 O 2 -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.
(© 2020 The Authors. New Phytologist © 2020 New Phytologist Trust.)
Databáze: MEDLINE
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