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Cited by 57RNA Research and SplicingRNA and protein synthesis mechanismsRNA regulation and disease

Molecular dissection of mRNA poly(A) tail length control in yeast

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Viphakone, Nicolas, Voisinet-Hakil, Florence, Minvielle-Sebastia, Lionel·2008·Nucleic Acids Research
DOI 10.1093/nar/gkn080PMC PMC2367721
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Abstract

In eukaryotic cells, newly synthesized mRNAs acquire a poly(A) tail that plays several fundamental roles in export, translation and mRNA decay. In mammals, PABPN1 controls the processivity of polyadenylation and the length of poly(A) tails during de novo synthesis. This regulation is less well-detailed in yeast. We have recently demonstrated that Nab2p is necessary and sufficient for the regulation of polyadenylation and that the Pab1p/PAN complex may act at a later stage in mRNA metabolism. Here, we show that the presence of both Pab1p and Nab2p in reconstituted pre-mRNA 3'-end processing reactions has no stimulating nor inhibitory effect on poly(A) tail regulation. Importantly, the poly(A)-binding proteins are essential to protect the mature mRNA from being subjected to a second round of processing. We have determined which domains of Nab2p are important to control polyadenylation and found that the RGG-box work in conjunction with the two last essential CCCH-type zinc finger domains. Finally, we have tried to delineate the mechanism by which Nab2p performs its regulation function during polyadenylation: it likely forms a complex with poly(A) tails different from a simple linear deposit of proteins as it has been observed with Pab1p.

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  • ERCC spike-ins have shorter poly(A) tails than typical mammalian mRNA, making them harder to capture by poly(T) priming.

    “On the one hand, ERCC spike-ins have shorter poly(A) tails than typical mRNA from mammalian cells10, making them harder to capture by poly(T) priming.”

    From Power analysis of single-cell RNA-sequencing experiments (2017) · cites this paper as [10]

  • ERCC spike-ins have short poly-A tails of 20 to 26 bases, mostly 24 bases, whereas eukaryotic mRNAs have poly-A tails of about 250 bases.

    “The ERCC spike-ins have short poly-A tails ranging from 20 to 26 bases long (the majority are 24 bases) in comparison to eukaryotic mRNAs of 250 base long poly-A tails10.”

    From Power analysis of single-cell RNA-sequencing experiments (2017) · cites this paper as [10]

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Authors
Viphakone, N., Voisinet-Hakil, F., & Minvielle-Sebastia, L.
Affiliations
Centre National de la Recherche Scientifique (FR)
ORCID
Viphakone, Nicolas
Venue
Nucleic Acids Research
Publisher
Oxford University Press (OUP)
Published
2008-02-26
Volume
36
Issue
7
Pages
2418-2433
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
DOI
10.1093/nar/gkn080
PMC
PMC2367721
OpenAlex
W2012097856
Cited by
57
References
53
Citations by year
2025: 2 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 3 · 2017: 5 · 2016: 4 · 2015: 1 · 2014: 3 · 2013: 6 · 2012: 8
FWCI
1.78
Type
journal article
Language
en
Open access
Licence
Locations
  • Nucleic Acids Research (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion)
  • HAL (submittedVersion)
Funders
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 › RNA regulation and disease
Keywords
polyadenylation, PABPN1, poly(A)-binding protein, RGG box, CCCH zinc finger, pre-mRNA 3' end processing, Saccharomyces cerevisiae, mRNA metabolism
MeSH terms
Poly A, Polynucleotide Adenylyltransferase, RNA, Fungal, Saccharomyces cerevisiae, Gene Expression Regulation, Fungal, Zinc Fingers, RNA-Binding Proteins, Protein Structure, Tertiary, 3' Untranslated Regions, Polyadenylation, Nucleocytoplasmic Transport Proteins, Saccharomyces cerevisiae Proteins, Poly(A)-Binding Proteins, Cytochromes c

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