Lazar G, Schaal T, Maniatis T, Goodman H M
Department of Molecular Biology, Massachusetts General Hospital, Boston 02114, USA.
Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7672-6. doi: 10.1073/pnas.92.17.7672.
We show that the higher plant Arabidopsis thaliana has a serine-arginine-rich (SR) protein family whose members contain a phosphoepitope shared by the animal SR family of splicing factors. In addition, we report the cloning and characterization of a cDNA encoding a higher-plant SR protein from Arabidopsis, SR1, which has striking sequence and structural homology to the human splicing factor SF2/ASF. Similar to SF2/ASF, the plant SR1 protein promotes splice site switching in mammalian nuclear extracts. A novel feature of the Arabidopsis SR protein is a C-terminal domain containing a high concentration of proline, serine, and lysine residues (PSK domain), a composition reminiscent of histones. This domain includes a putative phosphorylation site for the mitotic kinase cyclin/p34cdc2.
我们发现高等植物拟南芥拥有一个富含丝氨酸 - 精氨酸(SR)的蛋白家族,其成员含有动物SR剪接因子家族共有的磷酸化表位。此外,我们报道了从拟南芥中克隆和鉴定一个编码高等植物SR蛋白的cDNA,即SR1,它与人类剪接因子SF2/ASF具有显著的序列和结构同源性。与SF2/ASF相似,植物SR1蛋白在哺乳动物核提取物中促进剪接位点转换。拟南芥SR蛋白的一个新特征是其C末端结构域含有高浓度的脯氨酸、丝氨酸和赖氨酸残基(PSK结构域),这种组成让人联想到组蛋白。该结构域包括有丝分裂激酶细胞周期蛋白/p34cdc2的一个假定磷酸化位点。