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本文引用的文献

1
The yeast splicing factor Mud13p is a commitment complex component and corresponds to CBP20, the small subunit of the nuclear cap-binding complex.酵母剪接因子Mud13p是一种承诺复合体成分，相当于核帽结合复合体的小亚基CBP20。
Genes Dev. 1996 Jul 1;10(13):1699-708. doi: 10.1101/gad.10.13.1699.
2
A nuclear cap-binding complex facilitates association of U1 snRNP with the cap-proximal 5' splice site.一种核帽结合复合体促进U1小核核糖核蛋白颗粒（U1 snRNP）与帽近端5'剪接位点的结合。
Genes Dev. 1996 Jul 1;10(13):1683-98. doi: 10.1101/gad.10.13.1683.
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Nucleocytoplasmic transport.核质运输
Science. 1996 Mar 15;271(5255):1513-8. doi: 10.1126/science.271.5255.1513.
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An enhancer screen identifies a gene that encodes the yeast U1 snRNP A protein: implications for snRNP protein function in pre-mRNA splicing.一项增强子筛选鉴定出一个编码酵母U1 snRNP A蛋白的基因：对snRNP蛋白在前体mRNA剪接中的功能的启示。
Genes Dev. 1993 Mar;7(3):419-28. doi: 10.1101/gad.7.3.419.
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A nuclear cap binding protein complex involved in pre-mRNA splicing.一种参与前体信使核糖核酸剪接的核帽结合蛋白复合体。
Cell. 1994 Aug 26;78(4):657-68. doi: 10.1016/0092-8674(94)90530-4.
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Genetic and physical interactions between Srp1p and nuclear pore complex proteins Nup1p and Nup2p.Srp1p与核孔复合体蛋白Nup1p和Nup2p之间的遗传与物理相互作用。
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Yeast Srp1p has homology to armadillo/plakoglobin/beta-catenin and participates in apparently multiple nuclear functions including the maintenance of the nucleolar structure.酵母Srp1p与犰狳蛋白/桥粒斑珠蛋白/β-连环蛋白具有同源性，并参与明显多种核功能，包括核仁结构的维持。
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8
The yeast MUD2 protein: an interaction with PRP11 defines a bridge between commitment complexes and U2 snRNP addition.酵母MUD2蛋白：与PRP11的相互作用定义了前体复合物与U2 snRNP添加之间的桥梁。
Genes Dev. 1994 Apr 1;8(7):843-54. doi: 10.1101/gad.8.7.843.
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A cap-binding protein complex mediating U snRNA export.一种介导U小核RNA输出的帽结合蛋白复合体。
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Dynamic RNA-RNA interactions in the spliceosome.剪接体中的动态RNA-RNA相互作用。
Annu Rev Genet. 1994;28:1-26. doi: 10.1146/annurev.ge.28.120194.000245.

一种酵母帽结合蛋白复合体（yCBC）在mRNA前体剪接的早期步骤中发挥作用。

A yeast cap binding protein complex (yCBC) acts at an early step in pre-mRNA splicing.

作者信息

Lewis J D, Görlich D, Mattaj I W

机构信息

European Molecular Biology Laboratory, Heidelberg, Germany.

出版信息

Nucleic Acids Res. 1996 Sep 1;24(17):3332-6. doi: 10.1093/nar/24.17.3332.

DOI:10.1093/nar/24.17.3332
PMID:8811086
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC146107/
Abstract

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.

摘要

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。