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The Phtheirospermum japonicum isopentenyltransferase PjIPT1a regulates host cytokinin responses in Arabidopsis
Author(s) -
Greifenhagen Anne,
Braunstein Isabell,
Pfannstiel Jens,
Yoshida Satoko,
Shirasu Ken,
Schaller Andreas,
Spallek Thomas
Publication year - 2021
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/nph.17615
Subject(s) - haustorium , biology , arabidopsis , striga , parasitic plant , striga hermonthica , microbiology and biotechnology , arabidopsis thaliana , mutant , gene , transcriptome , nicotiana benthamiana , host (biology) , botany , genetics , gene expression , germination
Summary The hemiparasitic plant Phtheirospermum japonicum (Phtheirospermum) is a nutritional specialist that supplements its nutrient requirements by parasitizing other plants through haustoria. During parasitism, the Phtheirospermum haustorium transfers hypertrophy‐inducing cytokinins (CKs) to the infected host root. The CK biosynthesis genes required for haustorium‐derived CKs and the induction of hypertrophy are still unknown. We searched for haustorium‐expressed isopentenyltransferases (IPTs) that catalyze the first step of CK biosynthesis, confirmed the specific expression by in vivo imaging of a promoter‐reporter, and further analyzed the subcellular localization, the enzymatic function and contribution to inducing hypertrophy by studying CRISPR‐Cas9‐induced Phtheirospermum mutants. PjIPT1a was expressed in intrusive cells of the haustorium close to the host vasculature. PjIPT1a and its closest homolog PjIPT1b located to the cytosol and showed IPT activity in vitro with differences in substrate specificity. Mutating PjIPT1a abolished parasite‐induced CK responses in the host. A homolog of PjIPT1a also was identified in the related weed Striga hermonthica . With PjIPT1a, we identified the IPT enzyme that induces CK responses in Phtheirospermum japonicum‐ infected Arabidopsis roots. We propose that PjIPT1a exemplifies how parasitism‐related functions evolve through gene duplications and neofunctionalization.