A Cyclin-Dependent Kinase that Promotes Cytokinesis through Modulating Phosphorylation of the Carboxy Terminal Domain of the RNA Pol II Rpb1p Sub-Unit 英文参考文献.docVIP
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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 英文参考文献
ACyclin-DependentKinasethatPromotesCytokinesis
throughModulatingPhosphorylationoftheCarboxy
TerminalDomainoftheRNAPolIIRpb1pSub-Unit
JimKaragiannis1¤*,MohanK.Balasubramanian1,2
1LaboratoryofCell Division, TemasekLifeSciencesLaboratory, Singapore, Singapore,2Department of BiologicalSciences,NationalUniversityof
Singapore,Singapore,Singapore
In Schizosaccharomyces pombe, the nuclear-localized kinase, Lsk1p, promotes cytokinesis by positively regulating the
SeptationInitiationNetwork(SIN).Althoughamemberofthecyclin-dependentkinase(CDK)family,neitheracyclinpartner
nor a physiological target has been identified. In this report we identify a cyclin, Lsc1p, that physically interacts and co-
localizeswithLsk1p.Furthermore,lsk1D,lsc1D,aswellaskinase-deadlsk1-K306Rmutants,displayhighlysimilarcytokinesis
defects. Lsk1p is related to CDKs that phosphorylate the carboxy-terminal domain (CTD) of the largest sub-unit of RNA
polymeraseII(Rpb1p).Interestingly,wefindthatLsk1pandLsc1parerequiredforphosphorylationofSer-2residuesfoundin
theheptadrepeatsoftheCTD.TodetermineifRpb1pcouldbeaphysiologicaltarget,wereplacedthenativerpb1genewith
asyntheticgeneencodingaRpb1pproteininwhichSer-2wassubstitutedwiththenon-phosphorylatableamino-acidalanine
inallheptads.Cellscarryingthisalleleweresimilartolsk1Dmutants:Theywereviable,displayedgeneticinteractionswiththe
SIN, and were unable to complete cytokinesis upon perturbation of the cell division machinery. We conclude that Ser-2
phosphorylationoftheCTDheptadsplaysanovelphysiologicalroleintheregulationofcytokinesis.
Citation: KaragiannisJ,BalasubramanianMK(2007)ACyclin-DependentKinasethatPromotesCytokinesisthroughModulatingPhosphorylationof
theCarboxyTerminalDomainoftheRNAPolIIRpb1pSub-Unit.PLoSONE2(5):e433.doi:10.1371/journal.pone.0000433
INTRODUCTION
phosphorylation status of the CTD influences initiation and
elongationbythepolIIcomplex,aswellasthebindingofawide
variety of accessory factors required for the proper splicing,
capping,andpoly-a
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