Lewis J D, Görlich D, Mattaj I W
European Molecular Biology Laboratory, Heidelberg, Germany.
Nucleic Acids Res. 1996 Sep 1;24(17):3332-6. doi: 10.1093/nar/24.17.3332.
The function in splicing of a heterodimeric nuclear cap binding complex (yCBC) from the yeast Saccharomyces cerevisiae has been examined. Immunodepletion of splicing extracts with antibodies directed against one component of the complex, yCBP80, results in the efficient co-depletion of the second component, yCBP20, producing CBC-deficient splicing extract. This extract exhibits strongly reduced splicing efficiency and similar reductions in the assembly of both spliceosomes and of the earliest defined precursors to spliceosomes, commitment complexes. The addition of highly purified yCBC substantially restores these defects. These results, together with other data, suggest that CBCs play a highly conserved role in the recognition of pre-mRNA substrates at an early step in the splicing process.
对来自酿酒酵母的异二聚体核帽结合复合体(yCBC)在剪接中的功能进行了研究。用针对该复合体一个组分yCBP80的抗体对剪接提取物进行免疫去除,会导致另一个组分yCBP20的有效共去除,从而产生缺乏CBC的剪接提取物。这种提取物的剪接效率大幅降低,并且剪接体以及最早确定的剪接体前体(起始复合体)的组装也有类似程度的降低。添加高度纯化的yCBC可基本恢复这些缺陷。这些结果与其他数据表明,CBC在剪接过程的早期步骤中对前体mRNA底物的识别发挥着高度保守的作用。