PT  - JOURNAL ARTICLE
AU  - Maria Florencia Ercoli
AU  - Priscila Zonzini Ramos
AU  - Rashmi Jain
AU  - Joseph Pilotte
AU  - Oliver Xiaoou Dong
AU  - Ty Thompson
AU  - Carrow I. Wells
AU  - Jonathan M. Elkins
AU  - Aled M Edwards
AU  - Rafael M. Couñago
AU  - David H. Drewry
AU  - Pamela C. Ronald
TI  - An open source plant kinase chemogenomics set
AID  - 10.1101/2022.06.18.496431
DP  - 2022 Jan 01
TA  - bioRxiv
PG  - 2022.06.18.496431
4099  - http://biorxiv.org/content/early/2022/06/19/2022.06.18.496431.short
4100  - http://biorxiv.org/content/early/2022/06/19/2022.06.18.496431.full
AB  - 129 protein kinases, selected to represent the diversity of the rice (Oryza sativa) kinome, were cloned and tested for expression in E. coli. 40 of these rice kinases were purified and screened using differential scanning fluorimetry (DSF) against 627 diverse kinase inhibitors, with a range of structures and activities targeting diverse human kinases. 37 active compounds were then tested for their ability to modify primary root development in Arabidopsis. Of these, 14 compounds caused a significant reduction of primary root length and two slightly increased root elongation compared with control plants. Two inhibitory compounds bind to the predicted orthologue of Arabidopsis PSKR1, one of two receptors for PSK, a small sulfated peptide that positively controls root development. Inhibition could not be rescued by the exogenous addition of the PSK peptide, suggesting that chemical treatment may inhibit both PSKR1 and its closely related receptor PSKR2. Of the compounds acting as root growth inhibitors in Arabidopsis, six conferred the same effect in rice. Compound RAF265 (CHIR-265), previously shown to bind the human kinase BRAF (B-Raf proto-oncogene, serine/threonine kinase), also binds to nine highly conserved rice kinases tested. The binding of human and rice kinases to the same compound suggests that human kinase inhibitor sets will be useful for dissecting the function of plant kinases.Competing Interest StatementThe authors have declared no competing interest.