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    Wyświetlanie 1-7 z 7
    Tytuł:
    Cloning, expression, and crystallization of Cpn60 proteins from Thermococcus litoralis.
    Autorzy:
    Osipiuk, Jerzy
    Sriram, Mahalingam
    Mai, Xuhong
    Adams, Michael
    Joachimiak, Andrzej
    Powiązania:
    https://bibliotekanauki.pl/articles/1044434.pdf
    Data publikacji:
    2000
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    archaea
    chaperonin
    Thermococcus litoralis
    heat-shock protein
    Opis:
    Two genes of the extreme thermophilic archaeon Thermococcus litoralis homologous to those that code for Cpn60 chaperonins were cloned and expressed in Escherichia coli. Each of the Cpn60 subunits as well as the entire Cpn60 complex crystallize in a variety of morphological forms. The best crystals diffract to 3.6 Å resolution at room temperature and belong to the space group I422 with unit cell parameters a = b = 193.5 Å, c = 204.2 Å.
    Źródło:
    Acta Biochimica Polonica; 2000, 47, 1; 209-214
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    The GC-box is critical for high level expression of the testis-specific Hsp70.2/Hst70 gene
    Autorzy:
    Widłak, Wiesława
    Vydra, Natalia
    Dudaladava, Volha
    Ścieglińska, Dorota
    Winiarski, Bolesław
    Krawczyk, Zdzisław
    Powiązania:
    https://bibliotekanauki.pl/articles/1041120.pdf
    Data publikacji:
    2007
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Sp1
    GC-box
    regulation of gene expression
    spermatogenesis
    heat shock protein
    Opis:
    The Hsp70.2/Hst70 gene, which belongs to the 70 kDa heat-shock protein (HSP) family, is expressed specifically in primary spermatocytes and spermatids. The regulatory elements required for a high level of testis-specific expression of the gene are placed between the two major transcription start sites T1 and T2 (approximately 350 and 115 bp upstream of the starting ATG codon). Here we have shown that sequences proximal to the exon1/intron splicing site in the 5' untranslated region of the Hsp70.2/Hst70 gene, which include a highly conserved element called box B, are required for efficient expression of the chloramphenicol acetyltransferase reporter gene in testes of transgenic mice. However, in spite of the drastically reduced overall activity, the stage-specific expression pattern of the transgene was preserved after removal of these sequences. We have also shown that GC-box located downstream of the box B (approximately 210 bp upstream of the starting ATG codon) is indispensable for efficient expression of the Hsp70.2/Hst70 gene promoter in spermatogenic cells. The GC-box specifically binds proteins present in nuclear extracts from testes (putatively Sp1-like factors). A change in the pattern of such GC-box-interacting factors corresponds to activation of the Hsp70.2/Hst70 gene, confirming the importance of this regulatory element.
    Źródło:
    Acta Biochimica Polonica; 2007, 54, 1; 107-112
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Plasma membrane rafts and chaperones in cytokine/ STAT signaling.
    Autorzy:
    Sehgal, Pravin
    Powiązania:
    https://bibliotekanauki.pl/articles/1043429.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    cytokine receptors
    chaperones
    fever
    heat shock protein 90 (HSP90)
    signal transducers and activators of transciption (STATs)
    caveolin
    lipid rafts
    Opis:
    We and others have recently obtained data suggesting that cytokine-STAT signaling in many different cell-types is a chaperoned pathway initiated at the level of specialized plasma membrane microdomains called "rafts" (the "raft-STAT signaling hypothesis"). These findings are of broad significance in that all cytokines and growth factors initiate signaling in target cells by interacting with respective cell-surface receptors. The new data suggest that raft microdomains represent the units of function at the cell-surface through which ligand-stimulated STAT signaling is initiated. Moreover, recent evidence shows the involvement of chaperone proteins in regulating the STAT signaling pathway. These chaperones include the human homolog of the tumorous imaginal disc 1 protein (hTid1) which associates with Janus kinase 2 (JAK2) at the level of the plasma membrane, heat shock protein 90 (HSP90) which associates with STAT3 and STAT1 proteins in caveolin-1-containing raft and cytoplasmic complexes, and glucose regulated protein 58 (GRP58/ER-60/ERp57), a thiol dependent protein-disulfide isomerase, found in association with STAT3 "statosome" complexes in the cytosol and in the raft fraction. We suggest a function of the HSP90 chaperone system in preserving IL-6/STAT3 signaling in liver cells in the context of fever. The identification and function of protein partners associated with specific STAT species in rafts and in cytosolic complexes, and in the efficient departure of cytokine-activated STATs from the cytosolic face of rafts towards the cell nucleus are now areas of active investigation.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 3; 583-594
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Role of Escherichia coli heat shock proteins IbpA and IbpB in protection of alcohol dehydrogenase AdhE against heat inactivation in the presence of oxygen
    Autorzy:
    Matuszewska, Ewelina
    Kwiatkowska, Joanna
    Ratajczak, Elżbieta
    Kuczyńska-Wiśnik, Dorota
    Laskowska, Ewa
    Powiązania:
    https://bibliotekanauki.pl/articles/1040618.pdf
    Data publikacji:
    2009
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    AdhE
    protein aggregation
    protein oxidation
    small heat shock proteins IbpA and IbpB
    Opis:
    Escherichia coli small heat shock proteins IbpA and IbpB are molecular chaperones that bind denatured proteins and facilitate their subsequent refolding by the ATP-dependent chaperones DnaK/DnaJ/GrpE and ClpB. In vivo, the lack of IbpA and IbpB proteins results in increased protein aggregation under severe heat stress or delayed removal of aggregated proteins at recovery temperatures. In this report we followed the appearance and removal of aggregated alcohol dehydrogenase, AdhE, in E. coli submitted to heat stress in the presence of oxygen. During prolonged incubation of cells at 50°C, when AdhE was progressively inactivated, we initially observed aggregation of AdhE and thereafter removal of aggregated AdhE. In contrast to previous studies, the lack of IbpA and IbpB did not influence the formation and removal of AdhE aggregates. However, in ΔibpAB cells AdhE was inactivated and oxidized faster than in wild type strain. Our results demonstrate that IbpA and IbpB protected AdhE against thermal and oxidative inactivation, providing that the enzyme remained soluble. IbpA and IbpB were dispensable for the processing of irreversibly damaged and aggregated AdhE.
    Źródło:
    Acta Biochimica Polonica; 2009, 56, 1; 55-61
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Escherichia coli small heat shock proteins IbpA/B enhance activity of enzymes sequestered in inclusion bodies.
    Autorzy:
    Kuczyńska-Wiśnik, Dorota
    Żurawa-Janicka, Dorota
    Narkiewicz, Joanna
    Kwiatkowska, Joanna
    Lipińska, Barbara
    Laskowska, Ewa
    Powiązania:
    https://bibliotekanauki.pl/articles/1041504.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    protein aggregation
    inclusion bodies
    IbpA/B
    Opis:
    Escherichia coli small heat shock proteins, IbpA/B, function as molecular chaperones and protect misfolded proteins against irreversible aggregation. IbpA/B are induced during overproduction of recombinant proteins and bind to inclusion bodies in E. coli cells. We investigated the effect of ΔibpA/B mutation on formation of inclusion bodies and biological activity of enzymes sequestered in the aggregates in E. coli cells. Using three different recombinant proteins: Cro-β-galactosidase, β-lactamase and rat rHtrA1 we demonstrated that deletion of the ibpA/B operon did not affect the level of produced inclusion bodies. However, in aggregates containing IbpA/B a higher enzymatic activity was detected than in the IbpA/B-deficient inclusion bodies. These results confirm that IbpA/B protect misfolded proteins from inactivation in vivo.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 4; 925-931
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-7 z 7

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