role of plant-specific n-terminal domain of maize ck2β1 subunit in ck2β functions and holoenzyme regulation植物的n端结构域的作用的玉米在ck2βck2β1亚基函数和全酶调节.pdfVIP

Role of Plant-Specific N-Terminal Domain of Maize CK2b1 Subunit in CK2b Functions and Holoenzyme Regulation 1. 1. ´ ´ 1 1,2¤ Marta Riera , Sami Irar , Isabel C. Velez-Bermudez , Lorenzo Carretero-Paulet , Victoria 1 ` 1 Lumbreras , Montserrat Pages * 1 Department of Molecular Genetics, Centre for Research on Agricultural Genomics CRAG (CSIC-IRTA-UAB), Barcelona, Spain, 2 Department of Applied Biology (Area of ´ Genetics). University of Almerıa, Spain Abstract Protein kinase CK2 is a highly pleiotropic Ser/Thr kinase ubiquituous in eukaryotic organisms. CK2 is organized as a heterotetrameric enzyme composed of two types of subunits: the catalytic (CK2a) and the regulatory (CK2b). The CK2b subunits enhance the stability, activity and specificity of the holoenzyme, but they can also perform functions independently of the CK2 tetramer. CK2b regulatory subunits in plants differ from their animal or yeast counterparts, since they present an additional specific N-terminal extension of about 90 aminoacids that shares no homology with any previously characterized functional domain. Sequence analysis of the N-terminal domain of land plant CK2b subunit sequences reveals its arrangement through short, conserved motifs, some of them including CK2 autophosphorylation sites. By using maize CK2b1 and a deleted version (DNCK2b1) lacking the N-terminal domain, we have demonstrated that CK2b1 is autophosphorylated within the N-terminal domain. Moreover, the holoenzyme composed with CK2a1/DNCK2b1 is able to phosphorylate different substrates more efficiently