Valay J G, Dubois M F, Bensaude O, Faye G
Section de recherche, Institut Curie, Orsay, France.
C R Acad Sci III. 1996 Mar;319(3):183-9.
The Kin28 protein kinase interacts physically and genetically with cyclin Ccl1. Kin28 has been reported recently to be involved in the in vivo phosphorylation of the largest subunit of RNA polymerase II (Rpb1) in Saccharomyces cerevisiae. Now, we show that in a strain harboring a conditional ccl1-ts mutation, the C-terminal domain (CTD) of the Rpb1 subunit is under-phosphorylated at restrictive temperature. The transcription of a set of genes, chosen at random, is severely affected in a kin28-ts mutant shifted at restrictive temperature. Here, we report that the same set of genes requires a functional CCL1 gene product to be transcribed. These findings, added to previously published data, establishes that Kin28p is a cyclin-dependent kinase (CDK) with Ccl1p as a companion, both of them being necessary for general transcription and CTD phosphorylation.
Kin28蛋白激酶在物理和遗传上与细胞周期蛋白Ccl1相互作用。最近有报道称，Kin28参与酿酒酵母中RNA聚合酶II（Rpb1）最大亚基的体内磷酸化。现在，我们发现在携带条件性ccl1-ts突变的菌株中，Rpb1亚基的C末端结构域（CTD）在限制温度下磷酸化不足。在限制温度下转移的kin28-ts突变体中，一组随机选择的基因的转录受到严重影响。在此，我们报告同一组基因需要功能性CCL1基因产物才能转录。这些发现，加上先前发表的数据，证实Kin28p是一种细胞周期蛋白依赖性激酶（CDK），Ccl1p作为其伴侣，二者对于一般转录和CTD磷酸化都是必需的。
