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

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    Wyświetlanie 1-9 z 9
    Tytuł:
    Degradation of apoproteins of the major light harvesting complex of photosystem II (LHCII) in response to stresses is mediated by chloroplastic FtsH heterocomplex
    Autorzy:
    Lucinski, R.
    Jackowski, G.
    Powiązania:
    https://bibliotekanauki.pl/articles/81200.pdf
    Data publikacji:
    2013
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    conference
    apoprotein
    degradation
    light harvesting complex
    photosystem II
    chloroplast protein
    thylakoid membrane
    Arabidopsis thaliana
    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:
    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:
    Aggregation of LS Rubisco in response to exposure of plants to low irradiance
    Autorzy:
    Grabsztunowicz, M.
    Jackowski, G.
    Powiązania:
    https://bibliotekanauki.pl/articles/79910.pdf
    Data publikacji:
    2013
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    conference
    Rubisco
    aggregation
    bifunctional enzyme
    terrestrial plant
    holoenzyme
    reactive oxygen species
    oxidative modification
    plant exposure
    irradiance
    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:
    The regulatory role of AtDeg5 chloroplast protease in chronological progression of principal growth stages in Arabidopsis thaliana plants
    Autorzy:
    Baranek, M.
    Lucinski, R.
    Jackowski, G.
    Powiązania:
    https://bibliotekanauki.pl/articles/80598.pdf
    Data publikacji:
    2013
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    conference
    serine-type protease
    chymotrypsin
    thylakoid membrane
    photosystem II
    protease
    chloroplast
    Arabidopsis thaliana
    ontogenesis
    growth stage
    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:
    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:
    The contribution of individual domains of chloroplast protein AtDeg2 to its chaperone and proteolytic activities
    Autorzy:
    Jagodzik, P.
    Lucinski, R.
    Misztal, L.
    Jackowski, G.
    Powiązania:
    https://bibliotekanauki.pl/articles/59003.pdf
    Data publikacji:
    2018
    Wydawca:
    Polskie Towarzystwo Botaniczne
    Opis:
    The thylakoid protease AtDeg2 is a non-ATP hydrolyzing chloroplast protease/ chaperone peripherally connected with stromal side of thylakoid membrane. Its linear structure consists of protease domain and two PDZ domains. To unveil the significance of individual domains, chaperone and proteolytic activities of AtDeg2, its mutated recombinant versions have been developed and their ability to suppress protein aggregation and resolubilization of protein aggregates as well as the ability to degrade substrate protein was examined in vitro. Our work reveals for the first time that AtDeg2 is able not only to suppress aggregation of denatured proteins, but to resolubilize existing protein aggregates as well. We show that PDZ2 domain contributes significantly to both chaperone and protease activities of AtDeg2, whereas PDZ1 is required for chaperone but superfluous for proteolytic activity. Protease domain – but not S-268 in its catalytic site – contributes to chaperone activities of AtDeg2. These results show an entirely new function of AtDeg2 chaperone/protease (i.e., disaggregation of protein aggregates) and allow to identify structural motifs required for “old” and new functions of AtDeg2.
    Źródło:
    Acta Societatis Botanicorum Poloniae; 2018, 87, 1
    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 1-9 z 9

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