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001-es BibID:	BIBFORM131147
035-os BibID:	(Scopus)105009621773 (WoS)001528826900004
Első szerző:	Garda Tamás (biológus)
Cím:	Long-term treatments with microcystin-LR and diquat reveal their differences in the induction of oxidative stress responses and mitotic alterations in terms of stress recovery in Arabidopsis roots / Tamás Garda, Gabriella Petra Juhász, Adrienn Kelemen, Jaideep Mathur, László Ujlaky-Nagy, Csongor Freytag, Márta M-Hamvas, Milán Riba, Csaba Máthé
Dátum:	2025
ISSN:	0269-7491
Megjegyzések:	Microcystin-LR (MCY-LR), a widespread natural cyanobacterial toxin is a potent inhibitor of type 1 and 2A protein phosphatases (PP1, PP2A), inducing oxidative stress as well. Diquat (DQ) is a herbicide that inhibits electron transport to induce strong oxidative stress. Both compounds are affecting natural environments as well as plant and human health. We conducted a comparative analysis on their long-term (48 h) effects on reactive oxygen species (ROS) production, mitosis and histone H3 phosphorylation in root apical meristems of wild-type and PP2A-related mutants of Arabidopsis thaliana. MCY-LR did not increase ROS levels in any of the genotypes, but increased significantly the activity of ROS scavenging peroxidases (PODs) in Col0. DQ decreased ROS levels, but did not affect PODs. The paradoxical effect of DQ indicated the initiation of cell death processes. Mitosis was not affected by MCY-LR, but inhibited by DQ. Interestingly, MCY-LR as a phosphatase inhibitor did not affect histone H3 phosphorylation in mitotic cells, but DQ had an increasing effect. As we have shown previously, most of the above parameters changed differently at shorter (24 h) exposures: both compounds increased ROS levels in the phosphatase mutants, while POD activities were not affected; inhibition of mitosis or arrests in early mitosis, as well as increases of histone H3 phosphorylation levels occurred in the presence of both compounds. To conclude, Arabidopsis is able of recover partially and transiently from MCY-LR induced stress at long-term exposure, but this is not true for DQ. The environmental relevance of these findings is discussed.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Arabidopsis Microcystin-LR Diquat Oxidative stress Mitosis Histone H3 phosphorylation
Megjelenés:	Environmental Pollution. - 382 (2025), p. 1-10. -
További szerzők:	Juhász Gabriella Petra (1994-) (biologia tanár) Kelemen Adrienn (1995-) (Biológus) Mathur, Jaideep Ujlaky-Nagy László (1977-) (biofizikus) Freytag Csongor (1993-) (biológus) Mikóné Hamvas Márta (1963-) (biológus) Riba Milán (1990-) (biológus) Máthé Csaba (1966-) (biológus)
Pályázati támogatás:	120638 OTKA DETKA Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM073121
035-os BibID:	(WoS)000430302400011 (Scopus)85037678277
Első szerző:	Nagy Miklós (vegyész)
Cím:	Novel fluorochromes label tonoplast in living plant cells and reveal changes in vacuolar organization after treatment with protein phosphatase inhibitors / Nagy Miklós, Kéki Sándor, Rácz Dávid, Mathur Jaideep, Vereb György, Garda Tamás, M-Hamvas Márta, Chaumont Francois, Bóka Károly, Böddi Béla, Freytag Csongor, Vasas Gábor, Máthé Csaba
Dátum:	2018
ISSN:	0033-183X
Megjegyzések:	wavelengthsof around 366 nm and bind cysteine-rich proteins with hydrophobic motifs. We show that these compoundspreferentially label tonoplasts in living Arabidopsis and tobacco (Nicotiana tabacum SR1) cells. ACAIN-labeled membranesco-localized with the GFP signal in plants expressing GFP-?-TIP (TIP2;1) (a tonoplast aquaporin) fusion protein.ACAIN preserved the dynamics of vacuolar structures. tip2;1 and triple tip1;1-tip1;2-tip2;1 knockout mutants showedweaker ACAIN signal in tonoplasts. The fluorochrome is also suitable for the labeling and detection of specific(cysteine-rich, hydrophobic) proteins from crude cell protein extracts following SDS-PAGE and TIP mutants showaltered labeling patterns; however, it appears that ACAIN labels a large variety of tonoplast proteins. ACAIN/CACAIN could be used for the detection of altered vacuolar organization induced by the heptapeptide natural toxinmicrocystin-LR (MCY-LR), a potent inhibitor of both type 1 and 2A protein phosphatases and a ROS inducer. Asrevealed both in plants with GFP-TIP2;1 fusions and in wild-type (Columbia) plants labeled with ACAIN/CACAIN,MCY-LR induces the formation of small vesicles, concomitantly with the absence of the large vegetative vacuolescharacteristic for differentiated cells. TEM studies of MCY-LR-treated Arabidopsis cells proved the presence ofmultimembrane vesicles, with characteristics of lytic vacuoles or autophagosomes. Moreover, MCY-LR is a strongerinducer of small vesicle formation than okadaic acid (which inhibits preferentially PP2A) and tautomycin (which inhibitspreferentially PP1). ACAIN and CACAIN emerge as useful novel tools to study plant vacuole biogenesis and programmedcell death.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban ACAIN/CACAIN Arabidopsis Tonoplast Hypocotyl Microcystin-LR Vacuolar organization
Megjelenés:	Protoplasma. - 255 : 3 (2018), p. 829-839. -
További szerzők:	Kéki Sándor (1964-) (polimer kémikus) Rácz Dávid (1987-) (vegyész) Mathur, Jaideep Vereb György (1965-) (biofizikus, orvos) Garda Tamás (1990-) (biológus) Mikóné Hamvas Márta (1963-) (biológus) Chaumont, Francois Bóka Károly (1955-) (Biológus) Böddi Béla Freytag Csongor (1993-) (biológus) Vasas Gábor (1975-) (biológus-vegyész) Máthé Csaba (1966-) (biológus)
Pályázati támogatás:	116465 OTKA K-120638 OTKA GINOP-2.3.2-15-2016-00041 GINOP GINOP-2.3.3-15-2016-00030 GINOP Balassi Institute/Campus Hungary Mobility Support No. B2/2H/7717 Egyéb János Bolyai Research Scholarship MTA Discovery Grant from NSERC, Canada Egyéb
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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