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001-es BibID:	BIBFORM106511
035-os BibID:	(WoS)000995038700001 (Scopus)85147089622
Első szerző:	Freytag Csongor (biológus)
Cím:	B" and C subunits of PP2A regulate the levels of reactive oxygen species and superoxide dismutase activities in Arabidopsis / Csongor Freytag, Tamas Garda, Zoltan Konya, Marta M-Hamvas, Balazs Toth-Varady, Gabriella Petra Juhasz, Laszlo Ujlaky-Nagy, Adrienn Kelemen, Gabor Vasas, Csaba Mathe
Dátum:	2023
ISSN:	0981-9428
Megjegyzések:	The serine-threonine protein phosphatases PP2A regulate many cellular processes, however their role in oxidative stress responses and defence is less known. We show the involvement of its C (catalytic) and B" (a regulatory) subunits. The c3c4 (C subunit) and fass (B") subunit mutants and Col wt of Arabidopsis were used. Controls and treatments with the PP2A inhibitor microcystin-LR (MCY-LR) and reactive oxygen species (ROS) inducer diquat (DQ) were employed. ROS levels of primary roots were largely genotype dependent and both C and B" subunit mutants had increased sensitivity to MCY-LR and DQ indicating the involvement of these subunits in oxidative stress induction. Superoxide dismutases (SOD), mainly the Cu/Zn-SOD isoform, as key enzymes involved in ROS scavenging are also showing altered (mostly increased) activities in both c3c4 and fass mutants and have opposite relations to ROS induction. This indicates that the two types of subunits involved have partially different regulatory roles. In relation to this, control and MCY-LR/DQ treated B" subunit mutants were proven to have altered levels of phosphorylation of histone H2AX. γH2AX, the phosphorylated form indicates double stranded DNA damage during oxidative stress. Overall we point out the probable pivotal role of several PP2A subunits in the regulation of oxidative stress responses in plants and pave the way for future research to reveal the signaling pathways involved.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Protein phosphatase PP2A B" subunit C3C4 subunits Oxidative stress Phosphorylated H2AX Superoxide dismutase Cu/Zn-SOD
Megjelenés:	Plant Physiology And Biochemistry. - 195 (2023), p. 182-192. -
További szerzők:	Garda Tamás (1990-) (biológus) Kónya Zoltán (1986-) (molekuláris biológus, biokémikus) Mikóné Hamvas Márta (1963-) (biológus) Tóth-Várady Balázs Juhász Gabriella Petra (1994-) (biologia tanár) Ujlaky-Nagy László (1977-) (biofizikus) Kelemen Adrienn (1995-) (Biológus) Vasas Gábor (1975-) (biológus-vegyész) Máthé Csaba (1966-) (biológus)
Pályázati támogatás:	120638 OTKA 119647 OTKA ÚNKP-22-4-I-DE-11 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM122693
Első szerző:	Kelemen Adrienn (Biológus)
Cím:	Treatments with diquat reveal the relationship between protein phosphatases (PP2A) and oxidative stress during mitosis in Arabidopsis thaliana Root meristems / Adrienn Kelemen, Tamás Garda, Zoltán Kónya, Ferenc Erdődi, László Ujlaky-Nagy, Gabriella Petra Juhász, Csongor Freytag, Márta M-Hamvas, Csaba Máthé
Dátum:	2024
ISSN:	2223-7747
Megjegyzések:	Reversible protein phosphorylation regulates various cellular mechanisms in eukaryotes by altering the conformation, activity, localization, and stability of substrate proteins. In Arabidopsis thaliana root meristems, histone post-translational modifications are crucial for proper cell division, and they are also involved in oxidative stress signaling. To investigate the link between reactive oxygen species (ROS) and mitosis, we treated various Arabidopsis genotypes, including wild-types and mutants showing dysfunctional PP2A, with the ROS-inducing herbicide diquat (DQ). Studying the c3c4 double catalytic subunit mutant and fass regulatory subunit mutants of PP2A provided insights into phosphorylation-dependent mitotic processes. DQ treatment reduced mitotic activity in all genotypes and caused early mitotic arrest in PP2A mutants, likely due to oxidative stressinduced damage to essential mitotic processes. DQ had a minimal effect on reversible histone H3 phosphorylation in wild-type plants but significantly decreased phospho-histone H3 levels in PP2A mutants. Following drug treatment, the phosphatase activity decreased only in the stronger phenotype mutant plants (fass-5 and c3c4). Our findings demonstrate that (i) the studied PP2A loss-of-function mutants are more sensitive to increased intracellular ROS and (ii) DQ has indirect altering effects of mitotic activities and histone H3 phosphorylation. All these findings underscore the importance of PP2A in stress responses.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk protein phosphatases PP2A FASS C3-C4 histone H3 phosphorylation mitosis reactive oxygen species (ROS) Arabidopsis thaliana diquat
Megjelenés:	Plants-Basel. - 13 : 14 (2024), p. 1-16. -
További szerzők:	Garda Tamás (1990-) (biológus) Kónya Zoltán (1986-) (molekuláris biológus, biokémikus) Erdődi Ferenc (1953-) (biokémikus) Ujlaky-Nagy László (1977-) (biofizikus) Juhász Gabriella Petra (1994-) (biologia tanár) Freytag Csongor (1993-) (biológus) Mikóné Hamvas Márta (1963-) (biológus) Máthé Csaba (1966-) (biológus)
Pályázati támogatás:	OTKA-120638 OTKA ÚNKP-20-2-1-DE-129 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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