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

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    Wyświetlanie 1-4 z 4
    Tytuł:
    Isolation of intact and pure chloroplasts from leaves of Arabidopsis thaliana plants acclimated to low irradiance for studies on Rubisco regulation
    Autorzy:
    Grabsztunowicz, M.
    Jackowski, G.
    Powiązania:
    https://bibliotekanauki.pl/articles/56870.pdf
    Data publikacji:
    2013
    Wydawca:
    Polskie Towarzystwo Botaniczne
    Źródło:
    Acta Societatis Botanicorum Poloniae; 2013, 82, 1
    0001-6977
    2083-9480
    Pojawia się w:
    Acta Societatis Botanicorum Poloniae
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    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:
    Downregulation of chloroplast protease AtDeg5 leads to changes in chronological progression of ontogenetic stages, leaf morphology and chloroplast ultrastructure in Arabidopsis
    Autorzy:
    Baranek, M.
    Wyka, T.P.
    Jackowski, G.
    Powiązania:
    https://bibliotekanauki.pl/articles/57852.pdf
    Data publikacji:
    2015
    Wydawca:
    Polskie Towarzystwo Botaniczne
    Tematy:
    chloroplast protease
    AtDeg5 protease
    chronological progression
    ontogenetic stage
    leaf morphology
    chloroplast ultrastructure
    Arabidopsis
    starch grain
    Opis:
    The chloroplast protein AtDeg5 is a serine-type protease peripherally attached to thylakoid membrane at its lumenal side. Since reliable data regarding the role of AtDeg5 in controlling the course of growth and developmental processes are extremely limited, two independent T-DNA insertional lines with different extent of AtDeg5 reduction were prepared and ontogenesis stage-based analysis performed. Both mutant lines displayed a compensatory overaccumulation of AtDeg8. The repression of AtDeg5 protease altered a range of phenotypic features in at least one of the mutants, with the most prominent being changes in chronological progression of development and growth of individual rosette leaves, flower production and silique ripening as well as in the area of fully expanded leaves and chloroplast ultrastructure. By analyzing the results of parallel-mutant screening we conclude that AtDeg8 overdose may rescue 23% of AtDeg5 deficiency with regard to some AtDeg5-controlled traits; alternatively AtDeg5 may have catalytic sites in excess so that these traits might remain unaltered when AtDeg5 pool is reduced by 23%. For some other AtDeg5-dependent traits the absence of excessive amount of AtDeg5 catalytic sites, lack of AtDeg5 dosage effect and inability of AtDeg8 to compensate deficiency or absence of AtDeg5 occurred.
    Źródło:
    Acta Societatis Botanicorum Poloniae; 2015, 84, 1
    0001-6977
    2083-9480
    Pojawia się w:
    Acta Societatis Botanicorum Poloniae
    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 1-4 z 4

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