ArticleBiophysical journal2012
Nanopore detachment kinetics of poly(A) binding proteins from RNA molecules reveals the critical role of C-terminus interactions.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- mRNA poly(A)-tail length is a battleground for coronavirus-host competition.bioRxiv : the preprint server for biology · 2025Article
- The impact of mRNA poly(A) tail length on eukaryotic translation stages.Nucleic acids research · 2024Article
- Chemically Modified Poly(A) Analogs Targeting PABP: Structure Activity Relationship and Translation Inhibitory Properties.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Roles of mRNA poly(A) tails in regulation of eukaryotic gene expression.Nature reviews. Molecular cell biology · 2022Review
- The flip-flop configuration of the PABP-dimer leads to switching of the translation function.Nucleic acids research · 2022Article
- Different roles for the adjoining and structurally similar A-rich and poly(A) domains of oskar mRNA: Only the A-rich domain is required for oskar noncoding RNA function, which includes MTOC positioning.Developmental biology · 2021Article
- The molecular basis of coupling between poly(A)-tail length and translational efficiency.eLife · 2021Article
- Influenza A Virus NS1 Protein Binds as a Dimer to RNA-Free PABP1 but Not to the PABP1·Poly(A) RNA Complex.Biochemistry · 2020Article
- Impact of poly(A)-tail G-content on Arabidopsis PAB binding and their role in enhancing translational efficiency.Genome biology · 2019Article
- Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors.Nature communications · 2018Article
- Phosphorylation and interactions associated with the control of the Leishmania Poly-A Binding Protein 1 (PABP1) function during translation initiation.RNA biology · 2018Article
- Article
- The influence of microRNAs and poly(A) tail length on endogenous mRNA-protein complexes.Genome biology · 2017Article
- BTG2 bridges PABPC1 RNA-binding domains and CAF1 deadenylase to control cell proliferation.Nature communications · 2016Article
- Article
- Mimicking Ribosomal Unfolding of RNA Pseudoknot in a Protein Channel.Journal of the American Chemical Society · 2015Article
- Article
- Watching single proteins using engineered nanopores.Protein and peptide letters · 2014Review
- Detection of 3'-end RNA uridylation with a protein nanopore.ACS nano · 2014Article
- Poly(A) RNA and Paip2 act as allosteric regulators of poly(A)-binding protein.Nucleic acids research · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ubiquitous and abundant cytoplasmic poly(A) binding protein (PABP) is a highly conserved multifunctional protein, many copies of which bind to the poly(A) tail of eukaryotic mRNAs to promote translation initiation. The N-terminus of PABP is responsible for the high binding specificity and affinity to poly(A), whereas the C-terminus is known to stimulate PABP multimerization on poly(A). Here, we use single-molecule nanopore force spectroscopy to directly measure interactions between poly(A) and PABPs. Both electrical and biochemical results show that the C-C domain interaction between two consecutive PABPs promotes cooperative binding. Up to now, investigators have not been able to probe the detailed polarity configuration (i.e., the internal arrangement of two PABPs on a poly(A) streak in which the C-termini face toward or away from each other). Our nanopore force spectroscopy system is able to distinguish the cooperative binding conformation from the noncooperative one. The ∼50% cooperative binding conformation of wild-type PABPs indicates that the C-C domain interaction doubles the cooperative binding probability. Moreover, the longer dissociation time of a cooperatively bound poly(A)/PABP complex as compared with a noncooperatively bound one indicates that the cooperative mode is the most stable conformation for PABPs binding onto the poly(A). However, ∼50% of the poly(A)/PABP complexes exhibit a noncooperative binding conformation, which is in line with previous studies showing that the PABP C-terminal domain also interacts with additional protein cofactors.
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