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001-es BibID:BIBFORM027915
Első szerző:Gorovits, Rena
Cím:A mutation within the catalytic domain of COT1 kinase confers changes in the presence of two COT1 isoforms and in Ser/Thr protein kinase and phosphatase activities in Neurospora crassa / Rena Gorovits, Oshrat Propheta, Mikhail Kolot, Viktor Dombradi, Oded Yarden
Dátum:1999
Megjegyzések:Neurospora crassa grows by forming spreading colonies. cot-1 belongs to a class of N. crassa colonial temperature-sensitive (cot) mutants and encodes a Ser/Thr protein kinase. We have mapped the cot-1 mutation to a single base change resulting in a His to Arg substitution at amino acid 351, which resides within the catalytic domain. Antibodies raised against COT1 detected and immunoprecipitated a predominant 73-kDa polypeptide in N. crassa extracts, whose abundance was constant under all growth conditions tested. An additional, lower MW COT1 isoform (67-kDa) present in the wild-type was not detected in cot-1 grown at the restrictive temperature. Similarly, this isoform was not detected in cot-3 or cot-5 strains, when grown at restrictive temperatures. Reduced levels of Ser/Thr kinase activity and an increase in type 1 and type 2B phosphatase (calcineurin) activities were measured in a cot-1 background. Apparent changes in the phosphorylation state of the p150(Glued) subunit of the dynactin cytoskeletal motor component (encoded by ro-3, a suppressor of cot-1) and evidence of in vitro physical interactions between COT1 and calcineurin indicate a functional linkage among COT1 kinase, type 2B phosphatase, and dynactin.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
COT1
Ser/Thr protein kinase
Neurospora crassa
Megjelenés:Fungal Genetics and Biology. - 27 : 2-3 (1999), p. 264-274. -
További szerzők:Propheta, Oshrat Kolot, Mikhail Yarden, Oded Dombrádi Viktor (1953-) (biokémikus)
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2.

001-es BibID:BIBFORM036845
035-os BibID:PMID:22750657
Első szerző:Leiter Éva (biológus)
Cím:Protein phosphatase Z modulates oxidative stress response in fungi / Éva Leiter, Asier González, Éva Erdei, Carlos Casado, László Kovács, Csaba Ádám, Judit Oláh, Márton Miskei, Monika Molnar, Ilona Farkas, Zsuzsanna Hamari, Joaquín Ariño, István Pócsi, Viktor Dombrádi
Dátum:2012
ISSN:1087-1845
Megjegyzések:The genome of the filamentous fungus Aspergillus nidulans harbors the gene ppzA that codes for the catalytic subunit of protein phosphatase Z (PPZ), and the closely related opportunistic pathogen Aspergillus fumigatus encompasses a highly similar PPZ gene (phzA). When PpzA and PhzA were expressed in Saccharomyces cerevisiae or Schizosaccharomyces pombe they partially complemented the deleted phosphatases in the ppz1 or the pzh1 mutants, and they also mimicked the effect of Ppz1 overexpression in slt2 MAP kinase deficient S. cerevisiae cells. Although ppzA acted as the functional equivalent of the known PPZ enzymes its disruption in A. nidulans did not result in the expected phenotypes since it failed to affect salt tolerance or cell wall integrity. However, the inactivation of ppzA resulted in increased sensitivity to oxidizing agents like tert-butylhydroperoxide, menadione, and diamide. To demonstrate the general validity of our observations we showed that the deletion of the orthologous PPZ genes in other model organisms, such as S. cerevisiae (PPZ1) or Candida albicans (CaPPZ1) also caused oxidative stress sensitivity. Thus, our work reveals a novel function of the PPZ enzyme in A. nidulans that is conserved in very distantly related fungi.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Aspergillus (Emericella) nidulans
protein phosphatase Z
oxidative stress
tert-butylhydroperoxide
menadione
diamide
Molekuláris Medicina
egyetemen (Magyarországon) készült közlemény
Megjelenés:Fungal Genetics and Biology 49 : 9 (2012), p. 708-716. -
További szerzők:Gonzalez, Asier Erdei Éva (1983-) (biológus, biotechnológus) Casado, Carlos Kovács László (1982-) (Ph.D. hallgató, molekuláris biológus) Ádám Csaba (1980-) (molekuláris biológus) Oláh Judit Miskei Márton (1978-) (molekuláris biológus, genetikus) Molnár Mónika (biofizikus) Farkas Ilona (1953-) (biokémikus) Hamari Zsuzsanna Ariño, Joaquín Pócsi István (1961-) (vegyész) Dombrádi Viktor (1953-) (biokémikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
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