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Authordc.contributor.authorHinrichs, María V. 
Authordc.contributor.authorJedlicki, Ana 
Authordc.contributor.authorTellez, Rowena 
Authordc.contributor.authorPongor, Sándor 
Authordc.contributor.authorGatica, Marta 
Authordc.contributor.authorAllende, Catherine C. 
Authordc.contributor.authorAllende, Jorge E. 
Cita de ítemdc.identifier.citationBiochemistry, Volumen 32, Issue 28, 2018, Pages 7310-7316
Abstractdc.description.abstractCasein kinase II (CKII) is a ubiquitous protein kinase, found predominantly in cell nuclei, which has two subunits in a tetrameric α2β2 or αα′2 conformation. The catalytic center is present in the α subunit which is active by itself while β is a regulatory subunit that can greatly enhance the activity of α. The cDNA genes of Xenopus laevis coding for the α and β subunits of CKII have been expressed in Escherichia coli and extensively purified. The recombinant subunits reconstitute a fully active holoenzyme when incubated in stoichiometric amounts. Mutations that change serines in positions 2 and 3 of the β subunit for glycines completely eliminate the autophosphorylation site present in this subunit but do not significantly affect the capacity of β to activate α. A fusion protein composed of glutathione transferase linked to the X. laevis CKII β subunit can also activate α. This fusion protein binds to glutathione-agarose beads and can mediate the binding of the α subunit to this matri
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
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Títulodc.titleActivity of Recombinant α and β Subunits of Casein Kinase II from Xenopus laevis
Document typedc.typeArtículo de revista
Indexationuchile.indexArtículo de publicación SCOPUS

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Attribution-NonCommercial-NoDerivs 3.0 Chile
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile