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Structural insights into the assembly and polyA signal recognition mechanism of the human CPSF complex
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Structural insights into the assembly and polyA signal recognition mechanism of the human CPSF complex
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Journal Article
Structural insights into the assembly and polyA signal recognition mechanism of the human CPSF complex
2017
Overview
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.
Publisher
eLife Sciences Publications Ltd,eLife Sciences Publications, Ltd
Subject
/ Biochemistry and Chemical Biology
/ Cleavage And Polyadenylation Specificity Factor - chemistry
/ Cleavage And Polyadenylation Specificity Factor - metabolism
/ Humans
/ Lysine
/ mRNA
/ mRNA Cleavage and Polyadenylation Factors - chemistry
/ mRNA Cleavage and Polyadenylation Factors - metabolism
/ Nuclear Proteins - chemistry
/ Nuclear Proteins - metabolism
/ Protein Interaction Domains and Motifs
/ Proteins
/ Structural Biology and Molecular Biophysics
/ Sulfur
