a cyclin-dependent kinase that promotes cytokinesis through modulating phosphorylation of the carboxy terminal domain of the rna pol ii rpb1p sub-unit通过调节促进胞质分裂的细胞周期蛋白依赖性激酶磷酸化的羧基终端域rna聚合酶ii rpb1p单元.pdfVIP

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a cyclin-dependent kinase that promotes cytokinesis through modulating phosphorylation of the carboxy terminal domain of the rna pol ii rpb1p sub-unit通过调节促进胞质分裂的细胞周期蛋白依赖性激酶磷酸化的羧基终端域rna聚合酶ii rpb1p单元.pdf

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a cyclin-dependent kinase that promotes cytokinesis through modulating phosphorylation of the carboxy terminal domain of the rna pol ii rpb1p sub-unit通过调节促进胞质分裂的细胞周期蛋白依赖性激酶磷酸化的羧基终端域rna聚合酶ii rpb1p单元

A Cyclin-Dependent Kinase that Promotes Cytokinesis through Modulating Phosphorylation of the Carboxy Terminal Domain of the RNA Pol II Rpb1p Sub-Unit Jim Karagiannis1¤*, Mohan K. Balasubramanian1,2 1 Laboratory of Cell Division, Temasek Life Sciences Laboratory, Singapore, Singapore, 2 Department of Biological Sciences, National University of Singapore, Singapore, Singapore In Schizosaccharomyces pombe, the nuclear-localized kinase, Lsk1p, promotes cytokinesis by positively regulating the Septation Initiation Network (SIN). Although a member of the cyclin-dependent kinase (CDK) family, neither a cyclin partner nor a physiological target has been identified. In this report we identify a cyclin, Lsc1p, that physically interacts and co- localizes with Lsk1p. Furthermore, lsk1D, lsc1D, as well as kinase-dead lsk1-K306R mutants, display highly similar cytokinesis defects. Lsk1p is related to CDKs that phosphorylate the carboxy-terminal domain (CTD) of the largest sub-unit of RNA polymerase II (Rpb1p). Interestingly, we find that Lsk1p and Lsc1p are required for phosphorylation of Ser-2 residues found in the heptad repeats of the CTD. To determine if Rpb1p could be a physiological target, we replaced the native rpb1 gene with a synthetic gene encoding a Rpb1p protein in which Ser-2 was substituted with the non-phosphorylatable amino-acid alanine in all heptads. Cells carrying this allele were similar to lsk1D mutants: They were viable, displayed genetic interactions with the SIN, and were unable to complete cytokinesis upon perturbation of the cell division machinery. We conclude that Ser-2 phosphorylation of the CTD heptads plays a novel physiological role in the regulation of cytokinesis. Citation: Karagiannis J, Balasubramanian MK (2007) A Cyclin-Dependent Kinase that Promotes Cytokinesis through Modulating Phosphorylation of the Carboxy Terminal Doma