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    Wyświetlanie 1-4 z 4
    Tytuł:
    Doskonalenie ogórka (Cucumis sativus L.) pod względem odporności na kanciastą plamistość
    Improvement of cucumber (Cucumis sativus L.) in terms of angular leaf spot resistance
    Autorzy:
    Bartoszewski, Grzegorz
    Słomnicka, Renata
    Olczak-Woltman, Helena
    Korzeniewska, Aleksandra
    Gałecka, Teresa
    Kaźmińska, Karolina
    Niemirowicz-Szczytt, Katarzyna
    Powiązania:
    https://bibliotekanauki.pl/articles/2199518.pdf
    Data publikacji:
    2019-11-30
    Wydawca:
    Instytut Hodowli i Aklimatyzacji Roślin
    Tematy:
    Cucumis sativus L.
    P. syringae pv. lachrymans
    resistance
    QTL
    RNA-seq
    Źródło:
    Biuletyn Instytutu Hodowli i Aklimatyzacji Roślin; 2019, 286; 287-289
    0373-7837
    2657-8913
    Pojawia się w:
    Biuletyn Instytutu Hodowli i Aklimatyzacji Roślin
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Subcellular localization of UDP-GlcNAc, UDP-Gal and SLC35B4 transporters
    Autorzy:
    Maszczak-Seneczko, Dorota
    Olczak, Teresa
    Olczak, Mariusz
    Powiązania:
    https://bibliotekanauki.pl/articles/1039897.pdf
    Data publikacji:
    2011
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    MDCK-RCAr
    nucleotide sugar transporter
    Golgi apparatus
    endoplasmic reticulum
    Opis:
    The mechanisms of transport and distribution of nucleotide sugars in the cell remain unclear. In an attempt to further characterize nucleotide sugar transporters (NSTs), we determined the subcellular localization of overexpressed epitope-tagged canine UDP-GlcNAc transporter, human UDP-Gal transporter splice variants (UGT1 and UGT2), and human SLC35B4 transporter splice variants (longer and shorter version) by indirect immunofluorescence using an experimental model of MDCK wild-type and MDCK-RCAr mutant cells. Our studies confirmed that the UDP-GlcNAc transporter was localized to the Golgi apparatus only and its localization was independent of the presence of endogenous UDP-Gal transporter. After overexpression of UGT1, the protein colocalized with the Golgi marker only. When UGT2 was overexpressed, the protein colocalized with the endoplasmic reticulum (ER) marker only. When UGT1 and UGT2 were overexpressed in parallel, UGT1 colocalized with the ER and Golgi markers and UGT2 with the ER marker only. This suggests that localization of the UDP-Gal transporter may depend on the presence of the partner splice variant. Our data suggest that proteins involved in nucleotide sugar transport may form heterodimeric complexes in the membrane, exhibiting different localization which depends on interacting protein partners. In contrast to previously published data, both splice variants of the SLC35B4 transporter were localized to the ER, independently of the presence of endogenous UDP-Gal transporter.
    Źródło:
    Acta Biochimica Polonica; 2011, 58, 3; 413-419
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Analysis of individual azurocidin N-glycosylation sites in regard to its secretion by insect cells, susceptibility to proteolysis and antibacterial activity
    Autorzy:
    Indyk, Katarzyna
    Olczak, Teresa
    Ciuraszkiewicz, Justyna
    Wątorek, Wiesław
    Olczak, Mariusz
    Powiązania:
    https://bibliotekanauki.pl/articles/1041040.pdf
    Data publikacji:
    2007
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    glycosylation
    protein secretion
    azurocidin
    antimicrobial activity
    Opis:
    Azurocidin is an inactive serine protease homolog with primary sequence similarity to neutrophil elastase, cathepsin G, and proteinase 3. The aim of this study was to investigate possible consequences of differential glycosylation of azurocidin in regard to its secretion, protein stability as measured by susceptibility to proteolysis, and antibacterial activity. Site-directed mutagenesis was employed to generate mutant azurocidin variants lacking individual N-glycosylation sites. Our results show that N-linked glycans may play a role in proper azurocidin folding and subsequent secretion by insect cells. We also demonstrate that N-linked glycosylation contributes to azurocidin stability by protecting it from proteolysis. The lack of N-glycosylation at individual sites does not significantly influence the azurocidin antibacterial activity.
    Źródło:
    Acta Biochimica Polonica; 2007, 54, 3; 567-573
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Lysine-specific gingipain K and heme/hemoglobin receptor HmuR are involved in heme utilization in Porphyromonas gingivalis.
    Autorzy:
    Simpson, Waltena
    Olczak, Teresa
    Genco, Caroline
    Powiązania:
    https://bibliotekanauki.pl/articles/1043355.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Kgp
    heme
    Porphyromonas gingivalis
    HmuR
    gingipain
    Opis:
    We have previously reported on the identification and characterization of the Porphyromonas gingivalis A7436 strain outer membrane receptor HmuR, which is involved in the acquisition of hemin and hemoglobin. We demonstrated that HmuR interacts with the lysine- (Kgp) and arginine- (HRgpA) specific proteases (gingipains) and that Kgp and HRgpA can bind and degrade hemoglobin. Here, we report on the physiological significance of the HmuR-Kgp complex in heme utilization in P. gingivalis through the construction and characterization of a defined kgp mutant and a hmuR kgp double mutant in P. gingivalis A7436. The P. gingivalis kgp mutant exhibited a decreased ability to bind both hemin and hemoglobin. Growth of this strain with hemoglobin was delayed and its ability to utilize hemin as a sole iron source was diminished as compared to the wild type strain. Inactivation of both the hmuR and kgp genes resulted in further decreased ability of P. gingivalis to bind hemoglobin and hemin, as well as diminished ability to utilize either hemin or hemoglobin as a sole iron source. Collectively, these in vivo results further confirmed that both HmuR and Kgp are involved in the utilization of hemin and hemoglobin in P. gingivalis A7436.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 1; 253-262
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

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