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<dc:title xml:lang="en">Functional interactions of nuclear RNase P in Arabidopsis thaliana</dc:title>
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<dc:subject xml:lang="fr">ARN de transfert (ARNt)</dc:subject>
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<dcterms:abstract xml:lang="fr">La RNase P est une enzyme essentielle qui mature l’extrémité 5’ des précurseurs d’ARN de transfert. Ma thèse a visé à caractériser les interactions fonctionnelles de la RNase P nucléaire (PRORP2) chez Arabidopsis thaliana. Le réseau d’interaction protéine / protéine de PRORP2 a ainsi été déterminé, en démontrant que PRORP2 interagit fonctionnellement avec les tRNA methyltransférases 1A et 1B pour produire son activité sur les précurseurs d’ARNt. Ce résultat permet de mieux comprendre les étapes précoces de la maturation des ARNt chez les plantes. De plus, un nouveau substrat ARN de PRORP2 a été identifié. Il s’agit de l’ARN messager du gène MAF1 qui contient une structure ressemblant à un ARNt ou TLS pour « tRNA like structure ». Mes résultats démontrent que le TLS de MAF1 est un substrat in vitro et in vivo pour PRORP2. Ce qui permet de soutenir l’hypothèse que PRORP2 clive l’ARNm de MAF1, soit pour générer un nouveau petit ARN non codant, soit pour réguler le niveau d’expression du gène MAF1. MAF1 étant le principal régulateur négatif de l’ARN polymérase III, qui transcrit les ARNt, PRORP2 pourrait ainsi réguler indirectement l’activité de la polymérase III chez Arabidopsis thaliana.</dcterms:abstract>
<dcterms:abstract xml:lang="en">RNase P is an essential enzyme that maturates the 5’ leader sequence of tRNA precursors. My PhD project aimed at characterizing the functional interactions of nuclear RNase P (PRORP2) in Arabidopsis thaliana. The protein-protein network of interaction of PRORP2 was determined by co-immunoprecipitation and our results show that PRORP2 interacts with two tRNA methyltransferases (TRM1A and B) to properly maturate precursors tRNAs. This result gives new insights on the first steps of pre-tRNA processing in land plants. Moreover, a new RNA substrate of PRORP2 was discovered. It is a tRNA like structure (TLS) located in the messenger RNA of the MAF1 gene. My results show that MAF1 TLS is PRORP2 substrate in vitro and in vivo. This allow us to generate the hypothesis that PRORP2 cleaves MAF1 TLS, either to generate a new non-coding RNA or to regulate the level of expression of the MAF1 gene. As MAF1 is the main known negative regulator of RNA polymerase III (that transcribes tRNA), this could mean that PRORP2 regulates RNA pol. III activity in Arabidopsis thaliana.</dcterms:abstract>
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