Black C S, Garside E L, MacMillan A M, Rader S D
Department of Chemistry, University of Northern British Columbia, Prince George, British Columbia, V2N 4Z9, Canada.
Department of Biochemistry, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada.
Protein Sci. 2016 Apr;25(4):911-6. doi: 10.1002/pro.2894. Epub 2016 Feb 25.
Structural and functional analysis of proteins involved in pre-mRNA splicing is challenging because of the complexity of the splicing machinery, known as the spliceosome. Bioinformatic, proteomic, and biochemical analyses have identified a minimal spliceosome in the red alga Cyanidioschyzon merolae. This spliceosome consists of only 40 core proteins, compared to ∼ 70 in S. cerevisiae (yeast) and ∼ 150 in humans. We report the X-ray crystallographic analysis of C. merolae Snu13 (CmSnu13), a key component of the assembling spliceosome, and present evidence for conservation of Snu13 function in this algal splicing pathway. The near identity of CmSnu13's three-dimensional structure to yeast and human Snu13 suggests that C. merolae should be an excellent model system for investigating the structure and function of the conserved core of the spliceosome.
由于被称为剪接体的剪接机制十分复杂，对参与前体信使核糖核酸（pre-mRNA）剪接的蛋白质进行结构和功能分析颇具挑战性。生物信息学、蛋白质组学和生化分析已在红藻梅洛拟球藻（Cyanidioschyzon merolae）中鉴定出一种最小剪接体。与酿酒酵母（酵母）中的约70种及人类中的约150种相比，这种剪接体仅由40种核心蛋白质组成。我们报告了梅洛拟球藻Snu13（CmSnu13）的X射线晶体学分析，CmSnu13是组装剪接体的关键组分，并为该藻类剪接途径中Snu13功能的保守性提供了证据。CmSnu13的三维结构与酵母和人类Snu13近乎相同，这表明梅洛拟球藻应该是研究剪接体保守核心结构和功能的极佳模型系统。
