caa a22 4500 445318392 CHVBK 20180317142655.0 cr unu---uuuuu 170323e20110601xx s 000 0 eng 10.1007/s10126-010-9321-z doi (NATIONALLICENCE)springer-10.1007/s10126-010-9321-z Isolation of a CK2α Subunit and the Holoenzyme from the Mussel Mytilus galloprovincialis and Construction of the CK2α and CK2β cDNAs [Elektronische Daten] [Regina-Maria Kolaiti, Andrea Baier, Ryszard Szyszka, Sophia Kouyanou-Koutsoukou] Protein kinase CK2 is a ubiquitous, highly pleiotropic, and constitutively active phosphotransferase that phosphorylates mainly serine and threonine residues. CK2 has been studied and characterized in many organisms, from yeast to mammals. The holoenzyme is generally composed of two catalytic (α and/or α′) and two regulatory (β) subunits, forming a differently assembled tetramer. The free and catalytically active α/α′ subunits can be present in cells under some circumstances. We present here the isolation of a putative catalytic CK2α subunit and holoenzyme from gills of the mussel Mytilus galloprovincialis capable of phosphorylating the purified recombinant ribosomal protein rMgP1. For further analysis of M. galloprovincialis protein kinase CK2, the cDNA molecules of CK2α and CK2β subunits were constructed and cloned into expression vectors, and the recombinant proteins were purified after expression in Escherichia coli. The recombinant MgCK2β subunit and MgP1 were phosphorylated by the purified recombinant MgCK2α subunit. The mussel enzyme presented features typical for CK2: affinity for GTP, inhibition by both heparin and ATP competitive inhibitors (TBBt, TBBz), and sensitivity towards NaCl. Predicted amino acid sequence comparison showed that the M. galloprovincialis MgCK2α and MgCK2β subunits have similar features to their mammalian orthologs. Springer Science+Business Media, LLC, 2010 Protein kinase CK2 nationallicence Catalytic CK2α subunit nationallicence Regulatory CK2β subunit nationallicence Ribosomal stalk phosphorylation nationallicence Mytilus galloprovincialis nationallicence Kolaiti Regina-Maria Department of Genetics and Biotechnology, Faculty of Biology, University of Athens, Panepistimiopolis, 15701, Athens, Greece aut Baier Andrea Department of Molecular Biology, Institute of Biotechnology, The John Paul II Catholic University of Lublin, Al. Krasnicka 102, 20-718, Lublin, Poland aut Szyszka Ryszard Department of Molecular Biology, Institute of Biotechnology, The John Paul II Catholic University of Lublin, Al. Krasnicka 102, 20-718, Lublin, Poland aut Kouyanou-Koutsoukou Sophia Department of Genetics and Biotechnology, Faculty of Biology, University of Athens, Panepistimiopolis, 15701, Athens, Greece aut Marine Biotechnology Springer-Verlag 13/3(2011-06-01), 505-516 1436-2228 13:3<505 2011 13 10126 https://doi.org/10.1007/s10126-010-9321-z text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10126-010-9321-z text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kolaiti Regina-Maria Department of Genetics and Biotechnology, Faculty of Biology, University of Athens, Panepistimiopolis, 15701, Athens, Greece aut NATIONALLICENCE 700 1- Baier Andrea Department of Molecular Biology, Institute of Biotechnology, The John Paul II Catholic University of Lublin, Al. Krasnicka 102, 20-718, Lublin, Poland aut NATIONALLICENCE 700 1- Szyszka Ryszard Department of Molecular Biology, Institute of Biotechnology, The John Paul II Catholic University of Lublin, Al. Krasnicka 102, 20-718, Lublin, Poland aut NATIONALLICENCE 700 1- Kouyanou-Koutsoukou Sophia Department of Genetics and Biotechnology, Faculty of Biology, University of Athens, Panepistimiopolis, 15701, Athens, Greece aut NATIONALLICENCE 773 0- Marine Biotechnology Springer-Verlag 13/3(2011-06-01), 505-516 1436-2228 13:3<505 2011 13 10126 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer