Universität zu Köln

Nostadt, Robin, Hilbert, Magdalena, Nizam, Shadab, Rovenich, Hanna, Wawra, Stephan, Martin, Joerg, Kuepper, Hendrik, Mijovilovich, Ana, Ursinus, Astrid, Langen, Gregor ORCID: 0000-0002-8321-1756, Hartmann, Marcus D. ORCID: 0000-0001-6937-5677, Lupas, Andrei N. and Zuccaro, Alga ORCID: 0000-0002-8026-0114 (2020). A secreted fungal histidine- and alanine-rich protein regulates metal ion homeostasis and oxidative stress. New Phytol., 227 (4). S. 1174 - 1189. HOBOKEN: WILEY. ISSN 1469-8137

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Abstract

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 H2O2-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.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Nostadt, Robin UNSPECIFIED UNSPECIFIED UNSPECIFIED Hilbert, Magdalena UNSPECIFIED UNSPECIFIED UNSPECIFIED Nizam, Shadab UNSPECIFIED UNSPECIFIED UNSPECIFIED Rovenich, Hanna UNSPECIFIED UNSPECIFIED UNSPECIFIED Wawra, Stephan UNSPECIFIED UNSPECIFIED UNSPECIFIED Martin, Joerg UNSPECIFIED UNSPECIFIED UNSPECIFIED Kuepper, Hendrik UNSPECIFIED UNSPECIFIED UNSPECIFIED Mijovilovich, Ana UNSPECIFIED UNSPECIFIED UNSPECIFIED Ursinus, Astrid UNSPECIFIED UNSPECIFIED UNSPECIFIED Langen, Gregor UNSPECIFIED orcid.org/0000-0002-8321-1756 UNSPECIFIED Hartmann, Marcus D. UNSPECIFIED orcid.org/0000-0001-6937-5677 UNSPECIFIED Lupas, Andrei N. UNSPECIFIED UNSPECIFIED UNSPECIFIED Zuccaro, Alga UNSPECIFIED orcid.org/0000-0002-8026-0114 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-333662
DOI:	10.1111/nph.16606
Journal or Publication Title:	New Phytol.
Volume:	227
Number:	4
Page Range:	S. 1174 - 1189
Date:	2020
Publisher:	WILEY
Place of Publication:	HOBOKEN
ISSN:	1469-8137
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Biology > Botanical Institute
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language ENDOPHYTE PIRIFORMOSPORA-INDICA; SALIVARY PEPTIDE HISTATIN-5; SCHIZOSACCHAROMYCES-POMBE; SIDEROPHORE BIOSYNTHESIS; IRON ASSIMILATION; BINDING PROTEIN; LEUCINE-ZIPPER; PLANT DEFENSE; EFFECTOR; ZINC Multiple languages Plant Sciences Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/33366