Structure and Mechanism of Dimer-Monomer Transition of a Plant Poly(A)-Binding Protein upon RNA Interaction: Insights into Its Poly(A) Tail Assembly.
Identifieur interne : 000444 ( Main/Curation ); précédent : 000443; suivant : 000445Structure and Mechanism of Dimer-Monomer Transition of a Plant Poly(A)-Binding Protein upon RNA Interaction: Insights into Its Poly(A) Tail Assembly.
Auteurs : Mariane Noronha Domingues [Brésil] ; Mauricio Luis Sforça [Brésil] ; Adriana Santos Soprano [Brésil] ; Jack Lee [Royaume-Uni] ; Tatiana De Arruda Campos Brasil De Souza [Brésil] ; Alexandre Cassago [Brésil] ; Rodrigo Villares Portugal [Brésil] ; Ana Carolina De Mattos Zeri [Brésil] ; Mario Tyago Murakami [Brésil] ; Ari Sadanandom [Royaume-Uni] ; Paulo Sergio Lopes De Oliveira [Brésil] ; Celso Eduardo Benedetti [Brésil]Source :
- Journal of molecular biology [ 1089-8638 ] ; 2015.
English descriptors
- KwdEn :
- Amino Acid Sequence, Citrus sinensis (genetics), Citrus sinensis (metabolism), Kinetics, Models, Molecular, Molecular Sequence Data, Plant Proteins (chemistry), Plant Proteins (metabolism), Poly(A)-Binding Proteins (chemistry), Poly(A)-Binding Proteins (metabolism), Protein Binding, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Tertiary, RNA, Plant (chemistry), RNA, Plant (metabolism), RNA-Binding Proteins (chemistry), RNA-Binding Proteins (metabolism), Saccharomyces cerevisiae, Sequence Homology, Amino Acid.
- MESH :
- chemical , chemistry : Plant Proteins, Poly(A)-Binding Proteins, RNA, Plant, RNA-Binding Proteins.
- genetics : Citrus sinensis.
- metabolism : Citrus sinensis, Plant Proteins, Poly(A)-Binding Proteins, RNA, Plant, RNA-Binding Proteins.
- Amino Acid Sequence, Kinetics, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Tertiary, Saccharomyces cerevisiae, Sequence Homology, Amino Acid.
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.
DOI: 10.1016/j.jmb.2015.05.017
PubMed: 26013164
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pubmed:26013164Le document en format XML
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<author><name sortKey="Zeri, Ana Carolina De Mattos" sort="Zeri, Ana Carolina De Mattos" uniqKey="Zeri A" first="Ana Carolina De Mattos" last="Zeri">Ana Carolina De Mattos Zeri</name>
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<author><name sortKey="Murakami, Mario Tyago" sort="Murakami, Mario Tyago" uniqKey="Murakami M" first="Mario Tyago" last="Murakami">Mario Tyago Murakami</name>
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<author><name sortKey="Sadanandom, Ari" sort="Sadanandom, Ari" uniqKey="Sadanandom A" first="Ari" last="Sadanandom">Ari Sadanandom</name>
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<author><name sortKey="Oliveira, Paulo Sergio Lopes De" sort="Oliveira, Paulo Sergio Lopes De" uniqKey="Oliveira P" first="Paulo Sergio Lopes De" last="Oliveira">Paulo Sergio Lopes De Oliveira</name>
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<author><name sortKey="Benedetti, Celso Eduardo" sort="Benedetti, Celso Eduardo" uniqKey="Benedetti C" first="Celso Eduardo" last="Benedetti">Celso Eduardo Benedetti</name>
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<series><title level="j">Journal of molecular biology</title>
<idno type="eISSN">1089-8638</idno>
<imprint><date when="2015" type="published">2015</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Citrus sinensis (genetics)</term>
<term>Citrus sinensis (metabolism)</term>
<term>Kinetics</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Plant Proteins (chemistry)</term>
<term>Plant Proteins (metabolism)</term>
<term>Poly(A)-Binding Proteins (chemistry)</term>
<term>Poly(A)-Binding Proteins (metabolism)</term>
<term>Protein Binding</term>
<term>Protein Multimerization</term>
<term>Protein Structure, Quaternary</term>
<term>Protein Structure, Tertiary</term>
<term>RNA, Plant (chemistry)</term>
<term>RNA, Plant (metabolism)</term>
<term>RNA-Binding Proteins (chemistry)</term>
<term>RNA-Binding Proteins (metabolism)</term>
<term>Saccharomyces cerevisiae</term>
<term>Sequence Homology, Amino Acid</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plant Proteins</term>
<term>Poly(A)-Binding Proteins</term>
<term>RNA, Plant</term>
<term>RNA-Binding Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Citrus sinensis</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Citrus sinensis</term>
<term>Plant Proteins</term>
<term>Poly(A)-Binding Proteins</term>
<term>RNA, Plant</term>
<term>RNA-Binding Proteins</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Kinetics</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Protein Multimerization</term>
<term>Protein Structure, Quaternary</term>
<term>Protein Structure, Tertiary</term>
<term>Saccharomyces cerevisiae</term>
<term>Sequence Homology, Amino Acid</term>
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<front><div type="abstract" xml:lang="en">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.</div>
</front>
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