Maraia, R.J. & Intine, R.V. Recognition of nascent RNA by the human La antigen: conserved and diverged features of structure and function. Mol. Cell. Biol. 21, 367-379

阅读量:

30

作者:

RJ MaraiaRVA Intine

展开

摘要:

La is a conserved RNA-binding phosphoprotein that inter- acts with a large variety of ligands. The most ubiquitous func- tion of La is association with newly synthesized RNA polymer- ase (Pol) III transcripts via their common UUU-OH 39 termini and stabilization of these against exonucleolytic digestion. Ac- cumulating evidence also indicates an activity for La in internal ribosome entry site-mediated translation in mammalian cells and in the metabolism of a subset of 39-processed snRNA intermediates that end in uridylates but are synthesized by Pol II. The most highly conserved region of La resides in the N-terminal domain (NTD), and this appears to mediate high- affinity UUU-OH recognition. As critically reviewed here by comparison to a consensus core RNA recognition motif

展开

DOI:

10.1128/MCB.21.2.367-379.2001

被引量:

203

年份:

2001

通过文献互助平台发起求助,成功后即可免费获取论文全文。

相似文献

参考文献

引证文献

来源期刊

引用走势

2003
被引量:22

辅助模式

0

引用

文献可以批量引用啦~
欢迎点我试用!

引用