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    Wyświetlanie 1-5 z 5
    Tytuł:
    Developmental regulation of Ubc9 in the rat nervous system
    Autorzy:
    Watanabe, Mutsufusa
    Takahashi, Kaoru
    Tomizawa, Kayoko
    Mizusawa, Hidehiro
    Takahashi, Hiroshi
    Powiązania:
    https://bibliotekanauki.pl/articles/1040670.pdf
    Data publikacji:
    2008
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Ubc9
    SUMO
    in situ hybridization
    ubiquitin
    brain development
    Opis:
    The SUMO-conjugating enzyme Ubc9 is an essential enzyme in the SUMO (small ubiquitin-related modifier) protein modification system. Although sumoylation, covalent modification of cellular proteins by SUMO, is considered to regulate various cellular processes, and many substrates for sumoylation have been identified recently, the regulation of Ubc9 expression has not been examined in detail. We analyzed the expression of Ubc9 during rat brain development at the mRNA and protein levels. Northern and Western blot analyses revealed that expression of Ubc9 and SUMO-1 was developmentally regulated, while that of the ubiquitin-conjugating enzyme UbcH7 did not change so dramatically. In situ hybridization analysis revealed that the expression of Ubc9 was high in neuronal stem cells and moderate in differentiated neurons at embryonic stages. In the adult brain, moderate expression was observed in subsets of neurons, such as the dentate granular neurons and pyramidal neurons in the hippocampal formation and the large pyramidal neurons in the cerebral cortex. These results suggest that the Ubc9-SUMO system might participate in the proliferation and differentiation of neuronal cells in the developing brain and in neuronal plasticity in the adult brain.
    Źródło:
    Acta Biochimica Polonica; 2008, 55, 4; 681-686
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Rsp5 ubiquitin ligase affects isoprenoid pathway and cell wall organization in S. cerevisiae.
    Autorzy:
    Kamińska, Joanna
    Kwapisz, Marta
    Grabińska, Kariona
    Orłowski, Jacek
    Boguta, Magdalena
    Palamarczyk, Grażyna
    Żołądek, Teresa
    Powiązania:
    https://bibliotekanauki.pl/articles/1041478.pdf
    Data publikacji:
    2005
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Rsp5 ubiquitin ligase
    cell wall
    Mod5 tRNA: isopentenyltransferase
    ergosterol
    Opis:
    Dimethylallyl diphosphate, an isomer of isopentenyl diphosphate, is a common substrate of Mod5p, a tRNA modifying enzyme, and the farnesyl diphosphate synthase Erg20p, the key enzyme of the isoprenoid pathway. rsp5 mutants, defective in the Rsp5 ubiquitin-protein ligase, were isolated and characterized as altering the mitochondrial/cytosolic distribution of Mod5p. To understand better how competition for the substrate determines the regulation at the molecular level, we analyzed the effect of the rsp5-13 mutation on Erg20p expression. The level of Erg20p was three times lower in rsp5-13 compared to the wild type strain and this effect was dependent on active Mod5p. Northern blot analysis indicated a regulatory role of Rsp5p in ERG20 transcription. ERG20 expression was also impaired in pkc1Δ lacking a component of the cell wall integrity signaling pathway. Low expression of Erg20p in rsp5 cells was accompanied by low level of ergosterol, the main end product of the isoprenoid pathway. Additionally, rsp5 strains were resistant to nystatin, which binds to ergosterol present in the plasma membrane, and sensitive to calcofluor white, a drug destabilizing cell wall integrity by binding to chitin. Furthermore, the cell wall structure appeared abnormal in most rsp5-13 cells investigated by electron microscopy and chitin level in the cell wall was increased two-fold. These results indicate that Rsp5p affects the isoprenoid pathway which has important roles in ergosterol biosynthesis, protein glycosylation and transport and in this way may influence the composition of the plasma membrane and cell wall.
    Źródło:
    Acta Biochimica Polonica; 2005, 52, 1; 207-220
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Proteolityczny kombinat i jego regulatory
    The proteolytic machinery and its regulators
    Autorzy:
    Stój, J.
    Karpowicz, P.
    Powiązania:
    https://bibliotekanauki.pl/articles/171680.pdf
    Data publikacji:
    2012
    Wydawca:
    Polskie Towarzystwo Chemiczne
    Tematy:
    proteasom
    system ubikwityno-proteasomalny
    inhibitor
    allosteryczność
    proteasome
    ubiquitin-proteasome system
    allostery
    Opis:
    One of the proteolytic pathways existing in a cell is ubiquitin- proteasome system (UPS). This highly organized and ATP-dependent system is based on the multifunctional enzyme – the proteasome. Ubiquitin in this pathway plays a role of a tag which marks proteins intended for destruction. Ubiquitylated proteins are recognized and degraded by the 26S proteasome. It consists of a cylindrical-shaped proteolytic core – the proteasome 20S, and attached to it regulatory particles 19S (Fig. 2). The core is composed of four rings, each of them formed by seven subunits. The inner â-rings harbour active sites (in Eukaryota two of each kind: chymotrypsin-like (ChT-L), trypsin-like (T-L) and peptidylglutamyl (PGPH)). The outer, á-rings create a gated channel leading to the catalytic chamber [8]. In a latent proteasome the gate is closed by tightly packed N-terminal residues of á subunits (Fig. 4). Due to such architecture the active sites of the proteasome are not freely available for the substrates. An opening of the gate in physiological conditions occurs after binding the activators such as 11S, 19S or PA200. By catalysing degradation of proteins, the UPS is deeply involved in regulation of cellular physiology. It is also involved in removing of misfolded or damaged proteins and supports the immune system by generating antigenic peptides. Defects in functioning of this proteolytic system play a causal role in the development of a number of diseases, including inflammation, neurodegenerative diseases and various cancers [2–6] what is the reason why the proteasome has become an important therapeutic target. Detailed information about the structure, catalytic activities and mechanisms of functioning of the different proteasome complexes existing in cells is essential to understand their role in organisms as well as to develop new compounds which may find pharmaceutical application.
    Źródło:
    Wiadomości Chemiczne; 2012, 66, 11-12; 1097-1118
    0043-5104
    2300-0295
    Pojawia się w:
    Wiadomości Chemiczne
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    The role of Rsp5 ubiquitin ligase in regulation of diverse processes in yeast cells
    Autorzy:
    Kaliszewski, Paweł
    Żołądek, Teresa
    Powiązania:
    https://bibliotekanauki.pl/articles/1040663.pdf
    Data publikacji:
    2008
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Mga2
    ubiquitin ligase
    ubiquitination
    transcriptional activators
    Spt23
    Rsp5
    Saccharomyces cerevisiae
    Opis:
    Rsp5 is a conserved ubiquitin ligase involved in regulation of numerous cellular processes. A growing number of publications describing new functions of the ligase have appeared in recent years. Rsp5 was shown to be involved in the control of intracellular trafficking of proteins via endocytosis and multivesicular body sorting. Moreover, nuclear functions of Rsp5 in response to various stresses have been discovered. Rsp5 is also involved in the regulation of unsaturated fatty acid and sterol synthesis and phospholipid composition. Here, an overview of Rsp5 functions with emphasis on its involvement in the regulation of lipid biosynthesis will be presented.
    Źródło:
    Acta Biochimica Polonica; 2008, 55, 4; 649-662
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Immune signalling and vesicular trafficking – intertwining networks regulated by E3 ubiquitin ligases
    Autorzy:
    Stegmann, M.
    Furlan, G.
    Anderson, R.G.
    Ichimura, K.
    McDowell, J.M.
    Shirasu, K.
    Trujillo, M.
    Powiązania:
    https://bibliotekanauki.pl/articles/80842.pdf
    Data publikacji:
    2013
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    conference
    pattern recognition receptor
    pathogen-associated molecular pattern
    ubiquitin ligase
    subunit
    exocytosis
    immune response
    vesicular trafficking
    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
      Wyświetlanie 1-5 z 5

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