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Vannini, A.
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Vannini, A.
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show abstract
RNA polymerase I and III are responsible for the bulk of nuclear transcription in actively growing cells and their activity impacts the cellular biosynthetic capacity. As a consequence, RNA polymerase I and III deregulation has been directly linked to cancer development. The complexity of RNA polymerase I and III transcription apparatuses has hampered their structural characterization. However, in the last decade tremendous progresses have been made, providing insights into the molecular and functional architecture of these multi-subunit transcriptional machineries. Here we summarize the available structural data on RNA polymerase I and III, including specific transcription factors and global regulators. Despite the overall scarcity of detailed structural data, the recent advances in the structural biology of RNA polymerase I and III represent the first step towards a comprehensive understanding of the molecular mechanism underlying RNA polymerase I and III transcription. This article is part of a Special Issue entitled: Transcription by Odd Pols..
Vannini, A.
Cramer, P.
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Vol.45
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pp. 439-446.
show abstract
Recent studies of the three eukaryotic transcription machineries revealed that all initiation complexes share a conserved core. This core consists of the RNA polymerase (I, II, or III), the TATA box-binding protein (TBP), and transcription factors TFIIB, TFIIE, and TFIIF (for Pol II) or proteins structurally and functionally related to parts of these factors (for Pol I and Pol III). The conserved core initiation complex stabilizes the open DNA promoter complex and directs initial RNA synthesis. The periphery of the core initiation complex is decorated by additional polymerase-specific factors that account for functional differences in promoter recognition and opening, and gene class-specific regulation. This review outlines the similarities and differences between these important molecular machines..
Vannini, A.
Ringel, R.
Kusser, A.G.
Berninghausen, O.
Kassavetis, G.A.
Cramer, P.
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Cramer, P.
Armache, K.-.
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Brueckner, E.
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Dengl, S.
Geiger, S.R.
Jaslak, A.J.
Jawhari, A.
Jennebach, S.
Kamenski, T.
Kettenberger, H.
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Vannini, A.
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Vannini, A.
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Di Marco, S.
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Lorenzen, K.
Vannini, A.
Crarner, P.
Heck, A.J.
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Vannini, A.
Volpari, C.
Filocamo, G.
Casavola, E.C.
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Renzoni, D.
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Paolini, C.
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Steinkuhler, C.
Di Marco, S.
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Vannini, A.
Volpari, C.
Gargioli, C.
Muraglia, E.
Cortese, R.
De Francesco, R.
Neddermann, P.
Di Marco, S.
(2002). The crystal structure of the quorum sensing protein TraR bound to its autoinducer and target DNA. Embo journal,
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Abascal-Palacios, G.
Ramsay, E.P.
Beuron, F.
Morris, E.
Vannini, A.
Structural basis of RNA Polymerase III transcription initiation. Nature,
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