HIV-1 Pr55Gag binds genomic and spliced RNAs with different affinity and stoichiometry
Identifieur interne : 001D85 ( Main/Exploration ); précédent : 001D84; suivant : 001D86HIV-1 Pr55Gag binds genomic and spliced RNAs with different affinity and stoichiometry
Auteurs : Serena Bernacchi [France] ; Ekram W. Abd El-Wahab [France] ; Noé Dubois [France] ; Marcel Hijnen [Australie] ; Redmond P. Smyth [France] ; Johnson Mak [Australie] ; Roland Marquet [France] ; Jean-Christophe Paillart [France]Source :
- RNA Biology [ 1547-6286 ] ; 2016.
Descripteurs français
- KwdFr :
- ARN viral (), ARN viral (génétique), ARN viral (métabolisme), Cinétique, Conformation d'acide nucléique, Génome viral, Humains, Mutation, Protéines de liaison à l'ARN (métabolisme), Précurseurs de protéines (métabolisme), Sites de fixation, Séquences répétées inversées, VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (génétique), VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (métabolisme), Épissage des ARN.
- MESH :
- génétique : ARN viral, VIH-1 (Virus de l'Immunodéficience Humaine de type 1).
- métabolisme : ARN viral, Protéines de liaison à l'ARN, Précurseurs de protéines, VIH-1 (Virus de l'Immunodéficience Humaine de type 1).
- ARN viral, Cinétique, Conformation d'acide nucléique, Génome viral, Humains, Mutation, Sites de fixation, Séquences répétées inversées, Épissage des ARN.
English descriptors
- KwdEn :
- Binding Sites, Genome, Viral, HIV-1 (genetics), HIV-1 (metabolism), Humans, Inverted Repeat Sequences, Kinetics, Mutation, Nucleic Acid Conformation, Protein Precursors (metabolism), RNA Splicing, RNA, Viral (chemistry), RNA, Viral (genetics), RNA, Viral (metabolism), RNA-Binding Proteins (metabolism).
- MESH :
- chemical , chemistry : RNA, Viral.
- chemical , genetics : RNA, Viral.
- chemical , metabolism : Protein Precursors, RNA, Viral, RNA-Binding Proteins.
- genetics : HIV-1.
- metabolism : HIV-1.
- Binding Sites, Genome, Viral, Humans, Inverted Repeat Sequences, Kinetics, Mutation, Nucleic Acid Conformation, RNA Splicing.
Abstract
The HIV-1 Pr55Gag precursor specifically selects genomic RNA (gRNA) from a large variety of cellular and spliced viral RNAs (svRNAs), however the molecular mechanisms of this selective recognition remains poorly understood. To gain better understanding of this process, we analyzed the interactions between Pr55Gag and a large panel of viral RNA (vRNA) fragments encompassing the main packaging signal (Psi) and its flanking regions by fluorescence spectroscopy. We showed that the gRNA harbors a high affinity binding site which is absent from svRNA species, suggesting that this site might be crucial for selecting the HIV-1 genome. Our stoichiometry analysis of protein/RNA complexes revealed that few copies of Pr55Gag specifically associate with the 5′ region of the gRNA. Besides, we found that gRNA dimerization significantly impacts Pr55Gag binding, and we confirmed that the internal loop of stem-loop 1 (SL1) in Psi is crucial for specific interaction with Pr55Gag. Our analysis of gRNA fragments of different length supports the existence of a long-range tertiary interaction involving sequences upstream and downstream of the Psi region. This long-range interaction might promote optimal exposure of SL1 for efficient Pr55Gag recognition. Altogether, our results shed light on the molecular mechanisms allowing the specific selection of gRNA by Pr55Gag among a variety of svRNAs, all harboring SL1 in their first common exon.
Url:
DOI: 10.1080/15476286.2016.1256533
PubMed: 27841704
PubMed Central: 5270550
Affiliations:
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Le document en format XML
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<series><title level="j">RNA Biology</title>
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<term>Genome, Viral</term>
<term>HIV-1 (genetics)</term>
<term>HIV-1 (metabolism)</term>
<term>Humans</term>
<term>Inverted Repeat Sequences</term>
<term>Kinetics</term>
<term>Mutation</term>
<term>Nucleic Acid Conformation</term>
<term>Protein Precursors (metabolism)</term>
<term>RNA Splicing</term>
<term>RNA, Viral (chemistry)</term>
<term>RNA, Viral (genetics)</term>
<term>RNA, Viral (metabolism)</term>
<term>RNA-Binding Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ARN viral ()</term>
<term>ARN viral (génétique)</term>
<term>ARN viral (métabolisme)</term>
<term>Cinétique</term>
<term>Conformation d'acide nucléique</term>
<term>Génome viral</term>
<term>Humains</term>
<term>Mutation</term>
<term>Protéines de liaison à l'ARN (métabolisme)</term>
<term>Précurseurs de protéines (métabolisme)</term>
<term>Sites de fixation</term>
<term>Séquences répétées inversées</term>
<term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (génétique)</term>
<term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (métabolisme)</term>
<term>Épissage des ARN</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>RNA, Viral</term>
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<term>Précurseurs de protéines</term>
<term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1)</term>
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<term>Humans</term>
<term>Inverted Repeat Sequences</term>
<term>Kinetics</term>
<term>Mutation</term>
<term>Nucleic Acid Conformation</term>
<term>RNA Splicing</term>
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<term>Cinétique</term>
<term>Conformation d'acide nucléique</term>
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<term>Mutation</term>
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<front><div type="abstract" xml:lang="en"><title>ABSTRACT</title>
<p>The HIV-1 Pr55<sup>Gag</sup>
precursor specifically selects genomic RNA (gRNA) from a large variety of cellular and spliced viral RNAs (svRNAs), however the molecular mechanisms of this selective recognition remains poorly understood. To gain better understanding of this process, we analyzed the interactions between Pr55<sup>Gag</sup>
and a large panel of viral RNA (vRNA) fragments encompassing the main packaging signal (Psi) and its flanking regions by fluorescence spectroscopy. We showed that the gRNA harbors a high affinity binding site which is absent from svRNA species, suggesting that this site might be crucial for selecting the HIV-1 genome. Our stoichiometry analysis of protein/RNA complexes revealed that few copies of Pr55<sup>Gag</sup>
specifically associate with the 5′ region of the gRNA. Besides, we found that gRNA dimerization significantly impacts Pr55<sup>Gag</sup>
binding, and we confirmed that the internal loop of stem-loop 1 (SL1) in Psi is crucial for specific interaction with Pr55<sup>Gag</sup>
. Our analysis of gRNA fragments of different length supports the existence of a long-range tertiary interaction involving sequences upstream and downstream of the Psi region. This long-range interaction might promote optimal exposure of SL1 for efficient Pr55<sup>Gag</sup>
recognition. Altogether, our results shed light on the molecular mechanisms allowing the specific selection of gRNA by Pr55<sup>Gag</sup>
among a variety of svRNAs, all harboring SL1 in their first common exon.</p>
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<name sortKey="Abd El Wahab, Ekram W" sort="Abd El Wahab, Ekram W" uniqKey="Abd El Wahab E" first="Ekram W." last="Abd El-Wahab">Ekram W. Abd El-Wahab</name>
<name sortKey="Dubois, Noe" sort="Dubois, Noe" uniqKey="Dubois N" first="Noé" last="Dubois">Noé Dubois</name>
<name sortKey="Marquet, Roland" sort="Marquet, Roland" uniqKey="Marquet R" first="Roland" last="Marquet">Roland Marquet</name>
<name sortKey="Paillart, Jean Christophe" sort="Paillart, Jean Christophe" uniqKey="Paillart J" first="Jean-Christophe" last="Paillart">Jean-Christophe Paillart</name>
<name sortKey="Smyth, Redmond P" sort="Smyth, Redmond P" uniqKey="Smyth R" first="Redmond P." last="Smyth">Redmond P. Smyth</name>
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<country name="Australie"><noRegion><name sortKey="Hijnen, Marcel" sort="Hijnen, Marcel" uniqKey="Hijnen M" first="Marcel" last="Hijnen">Marcel Hijnen</name>
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<name sortKey="Mak, Johnson" sort="Mak, Johnson" uniqKey="Mak J" first="Johnson" last="Mak">Johnson Mak</name>
<name sortKey="Mak, Johnson" sort="Mak, Johnson" uniqKey="Mak J" first="Johnson" last="Mak">Johnson Mak</name>
<name sortKey="Mak, Johnson" sort="Mak, Johnson" uniqKey="Mak J" first="Johnson" last="Mak">Johnson Mak</name>
<name sortKey="Mak, Johnson" sort="Mak, Johnson" uniqKey="Mak J" first="Johnson" last="Mak">Johnson Mak</name>
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