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Wyszukujesz frazę "IbpA" wg kryterium: Temat


Wyświetlanie 1-3 z 3
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
Tytuł:
Expression in Escherichia coli of human ARHGAP6 gene and purification of His-tagged recombinant protein.
Autorzy:
Ochocka, Anna-Maria
Czyżewska, Marzena
Pawełczyk, Tadeusz
Powiązania:
https://bibliotekanauki.pl/articles/1043671.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
His-tag
IbpB
ARHGAP6
IbpA
Opis:
In this report we describe cloning and expression of human Rho GTPase activating protein (ARHGAP6) isoform 4 in Escherichia coli cells as a fusion protein with 6xHis. We cloned the ARHGAP6 cDNA into the bacterial expression vector pPROEX-1. Induction of the 6xHis-ARHGAP6 protein in BL21(DE3) and DH5α cells caused lysis of the cells irrespective of the kind of culture medium used. Successful expression of the fusion protein was obtained in the MC4100Δibp mutant strain lacking the small heat-shock proteins IbpA and IbpB. Reasonable yield was obtained when the cells were cultured in Terrific Broth + 1% glucose medium at 22°C for 16 h. The optimal cell density for expression of soluble 6xHis-ARHGAP6 protein was at A_600 about 0.5. Under these conditions over 90% of the fusion protein was present in a soluble form. The 6xHis-ARHGAP6 protein was purified to near homogeneity by a two step procedure comprising chromatography on Ni-nitrilotriacetate and cation exchange columns. The expression system and purification procedure employed made it possible to obtain 1-2 mg of pure 6xHis-ARHGAP6 protein from 300 ml (1.5 g of cells) of E. coli culture.
Źródło:
Acta Biochimica Polonica; 2003, 50, 1; 239-247
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
    Wyświetlanie 1-3 z 3

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