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不均一核核糖核蛋白复合物的C蛋白与聚腺苷酸化切割位点下游的RNA序列相互作用。

The C proteins of heterogeneous nuclear ribonucleoprotein complexes interact with RNA sequences downstream of polyadenylation cleavage sites.

作者信息

Wilusz J, Feig D I, Shenk T

机构信息

Department of Molecular Biology, Princeton University, New Jersey 08544.

出版信息

Mol Cell Biol. 1988 Oct;8(10):4477-83. doi: 10.1128/mcb.8.10.4477-4483.1988.

DOI:10.1128/mcb.8.10.4477-4483.1988
PMID:2847033
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC365522/
Abstract

The heterogeneous nuclear ribonucleoprotein C1 and C2 proteins were preferentially cross-linked by treatment with UV light in nuclear extracts to RNAs containing six different polyadenylation signals. The domain required for the interaction was located downstream of the poly(A) cleavage site, since deletion of this segment from several polyadenylation substrate RNAs greatly reduced cross-linking efficiency. In addition, RNAs containing only downstream sequences were efficiently cross-linked to C proteins, while fully processed, polyadenylated RNAs were not. Analysis of mutated variants of the simian virus 40 late polyadenylation signal showed that uridylate-rich sequences located in the region between 30 and 55 nucleotides downstream of the cleavage site were required for efficient cross-linking of C proteins. This downstream domain of the simian virus 40 late poly(A) addition signal has been shown to influence the efficiency of the polyadenylation reaction. However, there was not a strict correlation between cross-linking of C proteins and the efficiency of polyadenylation.

摘要

在核提取物中,用紫外线处理后,不均一核核糖核蛋白C1和C2蛋白优先与含有六种不同聚腺苷酸化信号的RNA发生交联。相互作用所需的结构域位于聚(A)切割位点的下游,因为从几种聚腺苷酸化底物RNA中缺失该片段会大大降低交联效率。此外,仅含有下游序列的RNA能有效地与C蛋白交联,而经过完全加工的聚腺苷酸化RNA则不能。对猿猴病毒40晚期聚腺苷酸化信号的突变变体分析表明,位于切割位点下游30至55个核苷酸区域内富含尿苷酸的序列是C蛋白有效交联所必需的。猿猴病毒40晚期聚(A)加尾信号的这个下游结构域已被证明会影响聚腺苷酸化反应的效率。然而,C蛋白的交联与聚腺苷酸化效率之间并没有严格的相关性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0474/365522/af6a0e8de7b8/molcellb00070-0519-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0474/365522/0b43ed827a28/molcellb00070-0516-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0474/365522/8e8b92073bcd/molcellb00070-0517-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0474/365522/7acafa251b3b/molcellb00070-0517-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0474/365522/fa3358b1b44c/molcellb00070-0518-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0474/365522/af6a0e8de7b8/molcellb00070-0519-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0474/365522/0b43ed827a28/molcellb00070-0516-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0474/365522/8e8b92073bcd/molcellb00070-0517-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0474/365522/7acafa251b3b/molcellb00070-0517-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0474/365522/fa3358b1b44c/molcellb00070-0518-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0474/365522/af6a0e8de7b8/molcellb00070-0519-a.jpg

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