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Wyszukujesz frazę "Jakubowicz, Teresa" wg kryterium: Autor


Wyświetlanie 1-7 z 7
Tytuł:
The effect of vanadate on Pichia pastoris growth, protein kinase A activity and ribosomal protein phosphorylation.
Autorzy:
Frajnt, Magdalena
Cytryńska, Małgorzata
Jakubowicz, Teresa
Powiązania:
https://bibliotekanauki.pl/articles/1043701.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein phosphorylation
vanadate
Pichia pastoris
PKA
ribosomal proteins
protein kinases
Opis:
It was found that wild type yeast Pichia pastoris can tolerate vanadate concentration as high as 25 mM in the growth medium. Moreover, four vanadate-resistant P. pastoris strains designated JC100/1, JC100/3, JC100/9 and JC100/15 exhibiting tolerance up to 150 mM vanadate were selected. Growth of P. pastoris was correlated with vanadate to vanadyl reduction and its accumulation in the growth medium. In two selected strains, JC100/9 and JC100/15, protein kinase A activity was much higher in comparison to the wild type strain even without vanadate addition to the growth medium. Moreover, in the presence of vanadate, protein kinase A activity was significantly increased in the wild type and the vanadate-resistant JC100/1 and JC100/3 strains. It was also found that phosphorylation of a 40 kDa protein associated with ribosomes occured in all vanadate-resistant strains from the logarithmic, while in the wild type strain from the stationary growth phase. From the presented results it can be concluded that a protein kinase A signalling pathway(s) might be involved in the mechanism of P. pastoris vanadate resistance. The results also indicate a possible role of the 40 kDa protein in protection of P. pastoris against vanadate toxicity.
Źródło:
Acta Biochimica Polonica; 2002, 49, 4; 959-968
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The effect of cAMP and cGMP on the activity and substrate specificity of protein kinase A from methylotrophic yeast Pichia pastoris.
Autorzy:
Frajnt, Magdalena
Cytryńska, Małgorzata
Jakubowicz, Teresa
Powiązania:
https://bibliotekanauki.pl/articles/1043395.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein phosphorylation
cAMP
PKA
cGMP
yeast
Opis:
Cyclic AMP dependent protein kinase (PKA) from Pichia pastoris yeast cells was found to be activated by either cAMP or cGMP. Analogs of cAMP such as 8-chloro-cAMP and 8-bromo-cAMP were as potent as cAMP in PKA activation while N6,2'-O-dibutyryl-cAMP did not stimulate the enzyme activity. It was shown that protamine sulfate was almost equally phosphorylated in the presence of 1-2 × 10-6 M cAMP or cGMP while other substrates such as Kemptide, ribosomal protein S6, were phosphorylated to a lower extent in the presence of cGMP. It was demonstrated that pyruvate kinase is a substrate of PKA which co-purified with the P. pastoris enzyme. Moreover, pyruvate kinase was phosphorylated by PKA in the presence of cAMP and cGMP to comparable levels.
Źródło:
Acta Biochimica Polonica; 2003, 50, 4; 1111-1118
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The involvement of protein kinase A in the immune response of Galleria mellonella larvae to bacteria
Autorzy:
Cytryńska, Małgorzata
Zdybicka-Barabas, Agnieszka
Jakubowicz, Teresa
Powiązania:
https://bibliotekanauki.pl/articles/1041132.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
antibacterial activity
protein kinase A
Rp-8-Br-cAMPS
lysozyme
Galleria mellonella
Opis:
The role of protein kinase A (PKA) in the humoral immune response of the greater wax moth Galleria mellonella larvae to live Gram-positive bacteria Micrococcus lysodeikticus and Gram-negative bacteria Escherichia coli was investigated. The immune challenge of larvae with both kinds of bacteria caused an increase in fat body PKA activity depending on the injected bacteria. Gram-positive M. lysodeikticus was a much better inducer of the enzyme activity than Gram-negative E. coli. The PKA activity was increased about 2.5-fold and 1.5-fold, after M. lysodeikticus and E. coli injection, respectively. The in vivo inhibition of the enzyme activity by a cell permeable selective PKA inhibitor, Rp-8-Br-cAMPS, was correlated with considerable changes of fat body lysozyme content and hemolymph antimicrobial activity in bacteria-challenged insects. The kinetics of changes were different and dependent on the bacteria used for the immune challenge of G. mellonella larvae.
Źródło:
Acta Biochimica Polonica; 2007, 54, 1; 167-174
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Phosphorylation of yeast ribosomal proteins by CKI and CKII in the presence of heparin
Autorzy:
Wojda, Iwona
Cytryńska, Małgorzata
Frajnt, Magdalena
Jakubowicz, Teresa
Powiązania:
https://bibliotekanauki.pl/articles/1044559.pdf
Data publikacji:
1999
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1999, 46, 1; 211-215
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Phosphorylation of acidic ribosomal proteins by ribosome-associated protein kinases of Saccharomyces cerevisiae and Schizosaccharofnyces pombe
Autorzy:
Jakubowicz, Teresa
Cytryńska, Małgorzata
Kowalczyk, Wiktor
Gąsior, Eugeniusz
Powiązania:
https://bibliotekanauki.pl/articles/1045441.pdf
Data publikacji:
1993
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1993, 40, 4; 497-505
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Protein kinases CKI and CKII are implicated in modification of ribosomal proteins of the yeast Trichosporon cutaneum
Autorzy:
Wojda, Iwona
Cytryńska, Małgorzata
Frajnt, Magdalena
Jakubowicz, Teresa
Powiązania:
https://bibliotekanauki.pl/articles/1043700.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
CKII
CKI
phosphorylation
ribosomal phosphoproteins
Trichosporon cutaneum
Opis:
Phosphorylation of acidic ribosomal proteins P1/P2-P0 is a common phenomenon in eukaryotic organisms. It was found previously that in Trichosporon cutaneum, unlike in other yeast species, in addition to the two acidic ribosomal proteins, two other proteins of 15 kDa and 19 kDa of the small ribosomal subunit were phosphorylated. Here we describe two protein kinases: CKI and CKII, which are engaged in the modification of T. cutaneum ribosomal proteins. The acidic ribosomal proteins and the protein of 19 kDa were modified by CKII associated with ribosomes, while the protein of 15 kDa was modified by CKI. Protein kinase CKI was purified from cell-free extract (CKIC) and from ribosomal fraction (CKIR). The molecular mass of CKIC was established at 33 kDa while that of CKIR at 35-37 kDa. A protein of 40 kDa copurified with CKIR but not CKIC. Heparin significantly increased 40 kDa protein phosphorylation level by CKIR. Microsequencing analysis revealed the presence of CKI recognition motifs in the N-terminal fragment of the 40 kDa protein.
Źródło:
Acta Biochimica Polonica; 2002, 49, 4; 947-957
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-7 z 7

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