Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

Wyszukujesz frazę "Jackowski, M." wg kryterium: Autor


Wyświetlanie 1-3 z 3
Tytuł:
AtDeg2 - a chloroplast protein with dual protease/chaperone activity
Autorzy:
Jagodzik, P.
Adamiec, M.
Jackowski, G.
Powiązania:
https://bibliotekanauki.pl/articles/57301.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Botaniczne
Tematy:
chloroplast protein
protease
proteolytic enzyme
chaperone
enzyme activity
chloroplast
PDZ domain
Opis:
Chloroplast protease AtDeg2 (an ATP-independent serine endopeptidase) is cytosolically synthesized as a precursor, which is imported into the chloroplast stroma and deprived of its transit peptide. Then the mature protein undergoes routing to its functional location at the stromal side of thylakoid membrane. In its linear structure AtDeg2 molecule contains the protease domain with catalytic triad (HDS) and two PDZ domains (PDZ1 and PDZ2). In vivo AtDeg2 most probably exists as a supposedly inactive haxamer, which may change its oligomeric stage to form active 12-mer, or 24-mer. AtDeg2 has recently been demonstrated to exhibit dual protease/chaperone function. This review is focused on the current awareness with regard to AtDeg2 structure and functional significance.
Źródło:
Acta Societatis Botanicorum Poloniae; 2014, 83, 3
0001-6977
2083-9480
Pojawia się w:
Acta Societatis Botanicorum Poloniae
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Dynamics of excitation energy transfer in PSII particles of Arabidopsis thaliana mutant clpC1
Autorzy:
Adamiec, M.
Lucinski, R.
Gibasiewicz, K.
Giera, W.
Sipinska, W.
Jackowski, G.
Powiązania:
https://bibliotekanauki.pl/articles/80441.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
excitation energy transfer
Arabidopsis thaliana
clpC1 mutant
polypeptide
time-resolved fluorescence
regulatory protein
chloroplast
apoprotein
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Chloroplast protease/chaperone AtDeg2 influences cotyledons opening and reproductive development in Arabidopsis
Autorzy:
Adamiec, M.
Jagodzik, P.
Wyka, T.P.
Ludwikow, A.
Mitula, F.
Misztal, L.
Lucinski, R.
Jackowski, G.
Powiązania:
https://bibliotekanauki.pl/articles/56435.pdf
Data publikacji:
2018
Wydawca:
Polskie Towarzystwo Botaniczne
Opis:
AtDeg2 is a chloroplast protein with dual protease/chaperone activity. Since data on how the individual activities of AtDeg2 affect growth and development of Arabidopsis thaliana plants is missing, two transgenic lines were prepared that express mutated AtDeg2 versions that have either only protease or chaperone activity and a comprehensive ontogenesis stage-based study was performed comprising wild type (WT) plants and insertional mutants that do not express AtDeg2, as well as the two transgenic lines. The repression of both AtDeg2 activities in deg2-3 mutants altered just a few phenotypic traits including the time when cotyledons were fully opened, the time when 10% flowers were open as well as the number of inflorescence branches and seed length in plants which have completed their generative development. It was demonstrated that complete opening of cotyledons as well as the number of inflorescence branches and seed length in plants which have completed their generative development required involvement of both AtDeg2 activities, whereas the time when 10% of flowers were open was controlled by AtDeg2 protease activity. These results show for the first time that the chaperone activity of AtDeg2 is needed for some elements of generative development of A. thaliana plants to proceed normally. So far, the chaperone activity of AtDeg2 was confirmed based on in vitro assays only.
Źródło:
Acta Societatis Botanicorum Poloniae; 2018, 87, 2
0001-6977
2083-9480
Pojawia się w:
Acta Societatis Botanicorum Poloniae
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

    Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies