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Structure and Mechanism of Dimer-Monomer Transition of a Plant Poly(A)-Binding Protein upon RNA Interaction: Insights into Its Poly(A) Tail Assembly

Domingues, M.N.; Sforça, M.L.; Soprano, A.S.; Lee, J.; Campos Brasil de Souza, T. de A.; Cassago, A.; Portugal, R.V.; de Mattos Zeri, A.C.; Murakami, M.T.; Sadanandom, A.; de Oliveira, P.S.; Benedetti, C.E.

Structure and Mechanism of Dimer-Monomer Transition of a Plant Poly(A)-Binding Protein upon RNA Interaction: Insights into Its Poly(A) Tail Assembly Thumbnail


Authors

M.N. Domingues

M.L. Sforça

A.S. Soprano

J. Lee

T. de A. Campos Brasil de Souza

A. Cassago

R.V. Portugal

A.C. de Mattos Zeri

M.T. Murakami

P.S. de Oliveira

C.E. Benedetti



Abstract

Poly(A)-binding proteins (PABPs) play crucial roles in mRNA biogenesis, stability, transport and translational control in most eukaryotic cells. Although animal PABPs are well-studied proteins, the biological role, three-dimensional structure and RNA-binding mode of plant PABPs remain largely uncharacterized. Here, we report the structural features and RNA-binding mode of a Citrus sinensis PABP (CsPABPN1). CsPABPN1 has a domain architecture of nuclear PABPs (PABPNs) with a single RNA recognition motif (RRM) flanked by an acidic N-terminus and a GRPF-rich C-terminus. The RRM domain of CsPABPN1 displays virtually the same three-dimensional structure and poly(A)-binding mode of animal PABPNs. However, while the CsPABPN1 RRM domain specifically binds poly(A), the full-length protein also binds poly(U). CsPABPN1 localizes to the nucleus of plant cells and undergoes a dimer–monomer transition upon poly(A) interaction. We show that poly(A) binding by CsPABPN1 begins with the recognition of the RNA-binding sites RNP1 and RNP2, followed by interactions with residues of the β2 strands, which stabilize the dimer, thus leading to dimer dissociation. Like human PABPN1, CsPABPN1 also seems to form filaments in the presence of poly(A). Based on these data, we propose a structural model in which contiguous CsPABPN1 RRM monomers wrap around the RNA molecule creating a superhelical structure that could not only shield the poly(A) tail but also serve as a scaffold for the assembly of additional mRNA processing factors.

Citation

Domingues, M., Sforça, M., Soprano, A., Lee, J., Campos Brasil de Souza, T. D. A., Cassago, A., …Benedetti, C. (2015). Structure and Mechanism of Dimer-Monomer Transition of a Plant Poly(A)-Binding Protein upon RNA Interaction: Insights into Its Poly(A) Tail Assembly. Journal of Molecular Biology, 427(15), 2491-2506. https://doi.org/10.1016/j.jmb.2015.05.017

Journal Article Type Article
Acceptance Date May 19, 2015
Online Publication Date Jul 31, 2015
Publication Date Jul 31, 2015
Deposit Date Sep 9, 2015
Publicly Available Date Jun 26, 2019
Journal Journal of Molecular Biology
Print ISSN 0022-2836
Publisher Elsevier
Peer Reviewed Peer Reviewed
Volume 427
Issue 15
Pages 2491-2506
DOI https://doi.org/10.1016/j.jmb.2015.05.017
Keywords CsPABPN1, Poly(A)-binding protein, RRM domain, Citrus sinensis, Dimer–monomer transition.

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