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001-es BibID:BIBFORM109570
035-os BibID:(cikkazonosító)586 (Scopus)85151426418 (WoS)000956870300001
Első szerző:Juhász Gabriella Petra (biologia tanár)
Cím:Microcystin-LR, a Cyanobacterial Toxin, Induces Changes in the Organization of Membrane Compartments in Arabidopsis / Gabriella Petra Juhász, Sándor Kéki, Anita Dékány-Adamoczky, Csongor Freytag, Gábor Vasas, Csaba Máthé, Tamás Garda
Dátum:2023
ISSN:2076-2607
Megjegyzések:To evaluate the effects of the cyanobacterial toxin microcystin-LR (MCY-LR, a protein phosphatase inhibitor) and diquat (DQ, an oxidative stress inducer) on the organization of tonoplast, the effect of MCY-LR on plastid stromule formation and on mitochondria was investigated in wildtype Arabidopsis. Tonoplast was also studied in PP2A catalytic (c3c4) and regulatory subunit mutants (fass-5 and fass-15). These novel studies were performed by CLSM microscopy. MCY-LR is produced during cyanobacterial blooms. The organization of tonoplast of PP2A mutants of Arabidopsis is much more sensitive to MCY-LR and DQ treatments than that of wild type. In c3c4, fass-5 and fass-15, control and treated plants showed increased vacuole fragmentation that was the strongest when the fass-5 mutant was treated with MCY-LR. It is assumed that both PP2A/C and B" subunits play an important role in normal formation and function of the tonoplast. In wild-type plants, MCY-LR affects mitochondria. Under the influence of MCY-LR, small, round-shaped mitochondria appeared, while long/fused mitochondria were typical in control plants. Presumably, MCY-LR either inhibits the fusion of mitochondria or induces fission. Consequently, PP2A also plays an important role in the fusion of mitochondria. MCY-LR also increased the frequency of stromules appearing on chloroplasts after 1 h treatments. Along the stromules, signals can be transported between plastids and endoplasmic reticulum. It is probable that they promote a faster response to stress.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Microorganisms. - 11 : 3 (2023), p. 1-13. -
További szerzők:Kéki Sándor (1964-) (polimer kémikus) Dékány-Adamoczky Anita (1985-) (anyagmérnök) Freytag Csongor (1993-) (biológus) Vasas Gábor (1975-) (biológus-vegyész) Máthé Csaba (1966-) (biológus) Garda Tamás (1990-) (biológus)
Pályázati támogatás:OTKA-120638
OTKA
OTKA-132685
OTKA
TKP2021-EGA-20
Egyéb
ÚNKP-22-4-I-DE-11
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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2.

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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