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001-es BibID:	BIBFORM027872
Első szerző:	Ayaydin, Ferhan
Cím:	Inhibition of serine/threonine-specific protein phosphatases causes premature activation of cdc2MsF kinase at G2/M transition and early mitotic microtubule organisation in alfalfa / Ferhan Ayaydin, Emese Vissi, Tamás Mészáros, Pál Miskolczi, Izabella Kovács, Attila Fehér, Viktor Dombrádi, Ferenc Erdődi, Pál Gergely, Dénes Dudits
Dátum:	2000
Megjegyzések:	Reversible phosphorylation of serine/threonine residues of cell cycle-regulatory proteins is one of the key molecular mechanisms controlling eukaryotic cell division. In plants, the protein kinase partners (i.e. p34cdc2/CDC28-related kinases) have been extensively studied, while the role of counter-acting protein phosphatases is less well understood. We used endothall (ET) as a cell-permeable inhibitor of serine/threonine-specific protein phosphatases to alter cytological and biochemical characteristics of cell division in cultured alfalfa cells. A high concentration of ET (10 and 50 microM) inhibited both protein phosphatases 1 and 2 (PP1 and PP2A), while a low concentration (1 microM) of ET-treatment primarily reduced the PP2A activity. High concentrations of the inhibitor increased the frequency of hypercondensed early and late prophase chromosomes that could not enter metaphase. In contrast, a low concentration of ET did not interfere with chromosomal events but caused significant alterations in the organisation of microtubules. Exposure of cells to 1 microM ET resulted in disturbance of preprophase band formation, increase in the number of nuclei with prophase microtubule assembly, premature polarisation of the spindle, and abnormal phragmoplast maturation. Under the same conditions, the ET-treated cells exhibited an early increase in cdc2MsF kinase activity. These results suggest that PP2A contributes to the control of mitotic kinase activities and microtubule organisation. Normal chromosome condensation and mitotic progression are dependent on both PP1 and PP2A activities. The presented data support the functional role of protein phosphatases in the co-ordination of chromosomal and microtubule events in dividing plant cells.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban serine/threonine phosphatases chromosome condensation preprophase band Cdc2-related kinase endothall Medicago sativa L egyetemen (Magyarországon) készült közlemény
Megjelenés:	The Plant Journal. - 23 : 1 (2000), p. 85-96. -
További szerzők:	Mészáros Tamás (Szeged) Miskolczi Pál (Szeged) Kovács Izabella (Szeged) Fehér Attila (Szeged) Dudits Dénes Vissi Emese (1968-) (biokémikus, biológus) Dombrádi Viktor (1953-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus) Gergely Pál (1947-) (biokémikus)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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001-es BibID:	BIBFORM030133
Első szerző:	Bíró Judit (Szeged)
Cím:	The histone phosphatase inhibitory property of plant nucleosome assembly protein-related proteins (NRPs) / Judit Bíró, Ilona Farkas, Mónika Domoki, Krisztina Ötvös, Sándor Bottka, Viktor Dombrádi, Attila Fehér
Dátum:	2012
ISSN:	0981-9428
Megjegyzések:	SET/I(2)(PP2A), a member of the family of nucleosome assembly proteins (NAPs), has been previously described as a multifunctional protein inhibiting protein phosphatase 2A (PP2A)-mediated histone H3((pSer10)) dephosphorylation during the heat shock response in animal cells. In the present work we demonstrate that its plant orthologs, designated as NAP-related proteins (NRPs), have a similar in vitro biochemical activity and interact with PP2A and histone H3((pSer10))in vivo. Although heat shock gene promoters were found to be associated with histone H3((pSer10))-marked chromatin following a high temperature treatment, heat shock gene expression was not affected in NRP-deficient mutant Arabidopsis thaliana (L.) plantlets. These observations indicate that NRPs are potential regulators of histone dephosphorylation in plants, but they are dispensable for gene expression reorganization in response to heat shock.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Plant Physiology And Biochemistry. - 52 (2012), p. 162-168. -
További szerzők:	Domoki Mónika (Szeged) Ötvös Krisztina (Szeged) Bottka Sándor Fehér Attila (Szeged) Farkas Ilona (1953-) (biokémikus) Dombrádi Viktor (1953-) (biokémikus)
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