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            <title xml:lang="en">Structural and biochemical studies on RNA polymerase elongation complexes bound to highly conserved transcription factors NusG and NusA</title>
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                <title xml:lang="en">Structural and biochemical studies on RNA polymerase elongation complexes bound to highly conserved transcription factors NusG and NusA</title>
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                <authority type="supervisor">Albert Weixlbaumer</authority>
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                <term xml:lang="en">Single particles cryo-EM</term>
                <term xml:lang="en">Dynamics of of the RNAP</term>
                <term xml:lang="en">NusG &amp; NusA</term>
                <term xml:lang="en">Transcription elongation &amp; termination</term>
                <term xml:lang="fr">La dynamique de l’ARNP</term>
                <term xml:lang="fr">Cryo-EM</term>
                <term xml:lang="fr">NusG &amp; NusA</term>
                <term xml:lang="fr">L’élongation &amp; la terminaison de la transcription</term>
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              <p>The RNAP (RNA polymerase) is the key enzyme in transcription. RNAP is tightly regulated by factors during transcriptional cycle. Two speed control transcriptional factors (TF) NusA and NusG have the opposite effect on transcriptional pausing. The aim of my work is to use single particle Cryo-EM combine with biochemistry analysis to bring out the regulation of NusA and NusG, and both TFs together on the RNAP. We demonstrate here that RNAP itsself has a constant dynamic movement – non-swiveled to swiveled conformation. NusA stabilized the RNAP to a swiveled conformation which close to the paused state, however NusG enhance the RNAP to an non-swiveled state. NusG-CTD compete with NusA on a same binding site, the Flap-Tip-Helix (FTH) module of RNAP. The biochemistry results showed that these two FT NusA and NusG, compensate the effect of each other and modulate the transcriptional rate in different transcriptional pausing context (class I and class II pausing). However at the termination rho-dependent context, NusA and NusG together could increase the termination efficiency at the terminator I site.</p>
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              <p>L'ARN-polymérase (ARNP) est l'enzyme clé de la transcription. Elle est étroitement régulée par des facteurs au cours du cycle de la transcription. Les deux facteurs NusA et NusG, ont un effet opposé sur la pause transcriptionnelle. Le but de ma thèse est d'utiliser la cryo-EM en analyse de particules isolées combinée à des analyses biochimiques pour mettre en évidence la régulation de l'ARNP par NusA et NusG, et ces deux facteurs ensemble. Nous démontrons que l'ARNP elle-même a un mouvement dynamique constant entre conformation non-pivotante et pivotante. NusA stabilise l'ARNP dans une conformation pivotante qui est proche de l'état de pause, alors que NusG favorise un état non-pivotant de l'ARNP. NusG-CTD est en compétition avec NusA sur un même site de liaison, le module Flap-Tip-Helix de l'ARNP. Les résultats biochimiques ont montré que NusA et NusG, compensent leurs effets et modulent la vitesse de transcription. Cependant, dans le contexte de la terminaison, rho-dépendante, NusA et NusG, ensemble pourraient augmenter l'efficacité de la terminaison précoce.</p>
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