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

ABSTRACT: Structural study of the polyA signal recognition by the human CPSF using X-ray crystallography, cross-linking MS, pull-downs and fluorescence polarisation assays.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Marco Faini

LAB HEAD: Ruedi Aebersold

PROVIDER: PXD008122 | Pride | 2017-12-18

REPOSITORIES: pride

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			Action	DRS
	Figure_1-Source_Data_1.xlsx	Xlsx
	mfaini_C1506_106.c.mzXML	Mzxml
	mfaini_C1506_107.c.mzXML	Mzxml
	mfaini_C1506_109.c.mzXML	Mzxml
	mfaini_C1506_110.c.mzXML	Mzxml

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Structural insights into the assembly and polyA signal recognition mechanism of the human CPSF complex.

Clerici Marcello M Faini Marco M Aebersold Ruedi R Jinek Martin M

eLife 20171223

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 ...[more]

PMID: 29274231

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