Počet záznamů: 1
Poly(ADP-ribose)-binding protein RCD1 is a plant PARylation reader regulated by Photoregulatory Protein Kinases
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SYSNO ASEP 0584196 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Poly(ADP-ribose)-binding protein RCD1 is a plant PARylation reader regulated by Photoregulatory Protein Kinases Tvůrce(i) Vainonen, J. P. (FI)
Gossens, R. (FI)
Krasensky-Wrzaczek, Julia (BC-A) RID, ORCID
De Masi, R. (DE)
Danciu, I. (AT)
Puukko, T. (FI)
Battchikova, N. (FI)
Jonak, C. (AT)
Wirthmueller, L. (DE)
Wrzaczek, Michael (BC-A) ORCID, RID, SAI
Shapiguzov, A. (FI)
Kangasjarvi, J. (FI)Celkový počet autorů 12 Číslo článku 429 Zdroj.dok. Communications Biology. - : Nature Publishing Group
Roč. 6, č. 1 (2023)Poč.str. 13 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova ubiquitination ; identification ; homeostasis ; immunity Vědní obor RIV EB - Genetika a molekulární biologie Obor OECD Biochemistry and molecular biology Způsob publikování Open access Institucionální podpora BC-A - RVO:60077344 UT WOS 000972469800004 EID SCOPUS 85152980330 DOI 10.1038/s42003-023-04794-2 Anotace Transcriptional regulation in plants through RADICAL-INDUCED CELL DEATH1 (RCD1) is controlled via its N-terminal domains and inhibitory phosphorylation by photoregulatory protein kinases (PPKs).
Poly(ADP-ribosyl)ation (PARylation) is a reversible post-translational protein modification that has profound regulatory functions in metabolism, development and immunity and is conserved throughout the eukaryotic lineage. Contrary to metazoa, many components and mechanistic details of PARylation have remained unidentified in plants. Here we present the transcriptional co-regulator RADICAL-INDUCED CELL DEATH1 (RCD1) as a plant PAR-reader. RCD1 is a multidomain protein with intrinsically disordered regions (IDRs) separating its domains. We have reported earlier that RCD1 regulates plant development and stress tolerance by interacting with numerous transcription factors (TFs) through its C-terminal RST domain. This study suggests that the N-terminal WWE and PARP-like domains, as well as the connecting IDR, play an important regulatory role in the RCD1 function. We show that RCD1 binds PAR in vitro via its WWE domain and that PAR-binding determines RCD1 localization to nuclear bodies (NBs) in vivo. Additionally, we found that RCD1 function and stability are controlled by Photoregulatory Protein Kinases (PPKs). PPKs localize with RCD1 in NBs and phosphorylate RCD1 at multiple sites affecting its stability. This work proposes a mechanism for negative transcriptional regulation in plants, in which RCD1 localizes to NBs, binds TFs with its RST domain and is degraded after phosphorylation by PPKs.Pracoviště Biologické centrum (od r. 2006) Kontakt Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Rok sběru 2024 Elektronická adresa https://www.nature.com/articles/s42003-023-04794-2
Počet záznamů: 1