剪接因子SRp20和9G8促进mRNA的核质输出。

Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA.

作者信息

Huang Y, Steitz J A

机构信息

Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06536, USA.

出版信息

Mol Cell. 2001 Apr;7(4):899-905. doi: 10.1016/s1097-2765(01)00233-7.

DOI:10.1016/s1097-2765(01)00233-7

PMID:11336712

Abstract

We have uncovered a novel function for two members of the SR protein family in mRNA export. Using UV cross-linking, transient transfection, and Xenopus oocyte microinjection, we find that the nucleocytoplasmic shuttling proteins SRp20 and 9G8 interact specifically with a 22-nt RNA element from the histone H2a gene to promote the export of intronless RNAs in both mammalian cells and Xenopus oocytes. Antibodies to SRp20 or 9G8 eliminate RNA binding and significantly inhibit the export of RNAs carrying the element from oocyte nuclei. Our observation that SRp20 and 9G8 can be UV cross-linked to polyadenylated RNA in both the nucleus and cytoplasm of HeLa cells suggests a more general role for these SR proteins in mRNA export.

摘要

我们发现了SR蛋白家族的两个成员在mRNA输出过程中的一种新功能。通过紫外线交联、瞬时转染和非洲爪蟾卵母细胞显微注射，我们发现核质穿梭蛋白SRp20和9G8与组蛋白H2a基因的一个22个核苷酸的RNA元件特异性相互作用，以促进无内含子RNA在哺乳动物细胞和非洲爪蟾卵母细胞中的输出。针对SRp20或9G8的抗体消除了RNA结合，并显著抑制携带该元件的RNA从卵母细胞核中输出。我们观察到SRp20和9G8在HeLa细胞核和细胞质中均可通过紫外线与多聚腺苷酸化RNA交联，这表明这些SR蛋白在mRNA输出中具有更广泛的作用。