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Kenesi, E.* ; Kolbert, Z.* ; Kaszler, N.* ; Klement,* ; Ménesi, D.* ; Molnár,* ; Valkai, I.* ; Feigl, G.* ; Rigó, G.* ; Cséplő,* ; Lindermayr, C. ; Fehér, A.*

ROP2 GTPase participates in nitric oxide (NO)-induced root shortening in arabidopsis.

Plants 12:17 (2023)
DOI PMC
Creative Commons Lizenzvertrag
Open Access Gold möglich sobald Verlagsversion bei der ZB eingereicht worden ist.
Nitric oxide (NO) is a versatile signal molecule that mediates environmental and hormonal signals orchestrating plant development. NO may act via reversible S-nitrosation of proteins during which an NO moiety is added to a cysteine thiol to form an S-nitrosothiol. In plants, several proteins implicated in hormonal signaling have been reported to undergo S-nitrosation. Here, we report that the Arabidopsis ROP2 GTPase is a further potential target of NO-mediated regulation. The ROP2 GTPase was found to be required for the root shortening effect of NO. NO inhibits primary root growth by altering the abundance and distribution of the PIN1 auxin efflux carrier protein and lowering the accumulation of auxin in the root meristem. In rop2-1 insertion mutants, however, wild-type-like root size of the NO-treated roots were maintained in agreement with wild-type-like PIN1 abundance in the meristem. The ROP2 GTPase was shown to be S-nitrosated in vitro, suggesting that NO might directly regulate the GTPase. The potential mechanisms of NO-mediated ROP2 GTPase regulation and ROP2-mediated NO signaling in the primary root meristem are discussed.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Arabidopsis Thaliana ; Pin1 ; Rho-type Small Gtpase ; S-nitrosation ; Auxin Transport ; Post-translational Modification ; Root Meristem; Induced Morphogenic Responses; S-nitrosylation; Auxin Transport; Growth; No; Stress; Colocalization; Trafficking; Proteins; Polarity
ISSN (print) / ISBN 2223-7747
e-ISSN 2223-7747
Zeitschrift Plants
Quellenangaben Band: 12, Heft: 4, Seiten: , Artikelnummer: 17 Supplement: ,
Verlag MDPI
Verlagsort Basel, Switzerland
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed