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PreprintCited by 6RNA Research and SplicingRNA and protein synthesis mechanismsProtein Structure and Dynamics

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Molecular details of the CPSF73-CPSF100 C-terminal heterodimer and interaction with Symplekin

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Thore, Stéphane, Raoelijaona, Finaritra, Talenton, Vincent, Fribourg, Sébastien, Mackereth, Cameron D.·2023·Open Biology
DOI 10.1101/2023.04.19.537554PMC PMC10688271

Preprint — published as 10.1098/rsob.230221 · Paper page

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Abstract

Eukaryotic pre-mRNA is processed by a large multiprotein complex to accurately cleave the 3’ end, and to catalyze the addition of the poly(A) tail. Within this cleavage and polyadenylation specificity factor (CPSF) machinery, the CPSF73 endonuclease subunit directly contacts both CPSF100 and the scaffold protein Symplekin to form a subcomplex known as the core cleavage complex (CCC) or mammalian cleavage factor (mCF). Here we have taken advantage of a stable CPSF73-CPSF100 minimal heterodimer from E. cuniculi to determine the solution structure formed by the first and second C-terminal domain (CTD1 and CTD2) of both proteins. We find a large number of contacts between both proteins in the complex, and notably in the region between CTD1 and CTD2. A similarity is also observed between CTD2 and the TATA-box binding protein (TBP) domains. Separately, we have determined the structure of the terminal CTD3 domain of CPSF73, which also belongs to the TBP domain family and is connected by a flexible linker to the rest of CPSF73. Biochemical assays demonstrate a key role for the CTD3 of CPSF73 in binding Symplekin, and structural models of the trimeric complex from other species allow for comparative analysis and support an overall conserved architecture.

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Metadata

Authors
Thore, S., Raoelijaona, F., Talenton, V., Fribourg, S., & Mackereth, C. D.
Affiliations
Centre National de la Recherche Scientifique (FR)
Corresponding author
  • Fribourg, Sébastien
  • Mackereth, Cameron D.
ORCID
Venue
Open Biology
Publisher
openRxiv
Published
2023-04-21
Volume
13
Issue
11
Pages
230221-230221
ISSN
2046-2441 (ISSN-L)
DOI
10.1101/2023.04.19.537554
PMC
PMC10688271
OpenAlex
W4388880407
Cited by
6
References
1
Citations by year
2026: 4 · 2024: 1 · 2023: 1
FWCI
0.53
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Open Biology (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • HAL (submittedVersion)
  • HAL (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Institut National de la Santé et de la Recherche Médicale
  • Centre National de la Recherche Scientifique
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
CPSF73, symplekin, cleavage and polyadenylation specificity factor, C-terminal domain, solution structure, Encephalitozoon cuniculi, protein-protein interaction, solution NMR
MeSH terms
Encephalitozoon cuniculi, mRNA Cleavage and Polyadenylation Factors, Cleavage And Polyadenylation Specificity Factor

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