4.8 Article

Structural insights in to the assembly and polyA signal recognition mechanism of the human CPSF complex

期刊

ELIFE
卷 6, 期 -, 页码 -

出版社

ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.33111

关键词

-

类别

资金

  1. European Research Council [ERC-StG-337284, HEALTH-F4-2008-201648, 233226]
  2. European Molecular Biology [ALTF-343-2013]
  3. H2020 European Research Council [670821]
  4. Innovative Medicines Initiative Joint Undertaking ULTRA-DD [115766]
  5. Howard Hughes Medical Institute

向作者/读者索取更多资源

3' polyadenylation is a key step in eukaryotic mRNA biogenesis. In mammalian cells, this process is dependent on the recognition of the hexanucleotide AAUAAA motif in the pre-mRNA polyadenylation signal by the cleavage and polyadenylation specificity factor (CPSF) complex. A core CPSF complex comprising CPSF160, WDR33, CPSF30 and Fip1 is sufficient for AAUAAA motif recognition, yet the molecular interactions underpinning its assembly and mechanism of PAS recognition are not understood. Based on cross-linking-coupled mass spectrometry, crystal structure of the CPSF160-WDR33 subcomplex and biochemical assays, we define the molecular architecture of the core human CPSF complex, identifying specific domains involved in inter-subunit interactions. In addition to zinc finger domains in CPSF30, we identify using quantitative RNA-binding assays an N-terminal lysine/arginine-rich motif in WDR33 as a critical determinant of specific AAUAAA motif recognition. Together, these results shed light on the function of CPSF in mediating PAS-dependent RNA cleavage and polyadenylation.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.8
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据