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1

Expression in Escherichia coli of human ARHGAP6 gene and purification of His-tagged recombinant protein

100%
Ochocka A. M., Czyzewska M., Pawelczyk T.
Acta Biochimica Polonica
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2003
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tom 50
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nr 1
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 DH5a 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 A600 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.
2
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Interplay between phosphoinositides and Ca2plus in phototropin1- and phototropin2-mediated chloroplast movements in Arabidopsis

84%
Aggarwal C., Labuz J., Gabrys H.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
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2013
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tom 94
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nr 3
3

Phosphatidylinositol 3-kinase-like activity in Tetrahymena. Effects of wortmannin and LY 294002

84%
Kovacs P., Pallinger E.
Acta Protozoologica
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2003
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tom 42
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nr 4
4
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Effect of triiodothyronine on the content of phospholipids in the rat liver nuclei

67%
Bucki R., Gorska M., Zendzian-Piotrowska M., Gorski J.
Journal of Physiology and Pharmacology
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2000
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tom 51
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nr 3
5

Surfactant proteins SP-A and SP-D in human health and disease

67%
Kishore U., Bernal A. L., Kamran M. F., Saxena S., Singh M., Sarma P. U., Madan T., Chakraborty T.
Archivum Immunologiae et Therapiae Experimentalis
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2005
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tom 53
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nr 5
6

Assessment of mechanisms involved in regulation of the primate corpus luteum

67%
Ottobre J. S., Ciereszko R. E., Houmard B. S.
Journal of Physiology and Pharmacology. Supplement
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1996
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tom 47
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nr 1
7
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Stimulation of arachidonic acid release from thyroid phospholipids

67%
Stelmach H., Jaroszewicz L.
Journal of Physiology and Pharmacology
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1995
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tom 46
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nr 4
8

Investigation of interaction of human platelet membrane components with anticoagulant drugs abciximab and eptifibatide

59%
Gorodkiewicz E., Sankiewicz A., Figaszewski Z.
Folia Histochemica et Cytobiologica
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2010
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tom 48
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nr 4
9

Regulation of wound-responsive calcium-dependent protein kinase from maize (ZmCPK11) by phosphatidic acid

59%
Klimecka M., Szczegielniak J., Godecka L., Lewandowska-Gnatowska E., Dobrowolska G., Muszynska G.
Acta Biochimica Polonica
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2011
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tom 58
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nr 4
In plant cells, phospholipids are not only membrane components but also act as second messengers interacting with various proteins and regulating diverse cellular processes, including stress signal transduction. Here, we report studies on the effects of various phospholipids on the activity and expression of maize wound-responsive calcium-dependent protein kinase (ZmCPK11). Our results revealed that in leaves treated with n-butanol, a potent inhibitor of phosphatidic acid (PA) synthesis catalyzed by phospholipase D, a significant decrease of ZmCPK11 activity was observed, indicating contribution of PA in the kinase activation. Using lipid binding assays, we demonstrate that among various phospholipids only saturated acyl species (16 : 0 and 18 : 0) of phosphatidic acid are able to bind to ZmCPK11. Saturated acyl species of PA are also able to stimulate phosphorylation of exogenous substrates by ZmCPK11 and autophosphorylation of the kinase. The level of ZmCPK11 autophosphorylation is correlated with its enzymatic activity. RT-PCR analysis showed that transcript level of ZmCPK11 in maize leaves increased in response to PA treatment. The influence of PA on the activity and transcript level of ZmCPK11 suggests an involvement of this kinase in a PA-mediated wound signal transduction pathway.
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