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Instruments / Technical Area	Publication Details	Published	Actions
Krios III-Titan Krios III at Diamond Krios IV-Titan Krios IV at Diamond	Structural basis of RNA polymerase inhibition by viral and host factors Simona Pilotto , Thomas Fouqueau , Natalya Lukoyanova , Carol Sheppard , Soizick Lucas-Staat , Luis Miguel Diaz-Santin , Dorota Matelska , David Prangishvili , Alan C. M. Cheung , Finn Werner Nature Communications 12 DOI: 10.1038/s41467-021-25666-5 Diamond Proposal Number(s): [20287] Open Access Show Abstract ▼ Abstract: RNA polymerase inhibition plays an important role in the regulation of transcription in response to environmental changes and in the virus-host relationship. Here we present the high-resolution structures of two such RNAP-inhibitor complexes that provide the structural bases underlying RNAP inhibition in archaea. The Acidianus two-tailed virus encodes the RIP factor that binds inside the DNA-binding channel of RNAP, inhibiting transcription by occlusion of binding sites for nucleic acid and the transcription initiation factor TFB. Infection with the Sulfolobus Turreted Icosahedral Virus induces the expression of the host factor TFS4, which binds in the RNAP funnel similarly to eukaryotic transcript cleavage factors. However, TFS4 allosterically induces a widening of the DNA-binding channel which disrupts trigger loop and bridge helix motifs. Importantly, the conformational changes induced by TFS4 are closely related to inactivated states of RNAP in other domains of life indicating a deep evolutionary conservation of allosteric RNAP inhibition.	Sep 2021
Krios I-Titan Krios I at Diamond Krios II-Titan Krios II at Diamond	A tail-based mechanism drives nucleosome demethylation by the LSD2/NPAC multimeric complex Chiara Marabelli , Biagina Marrocco , Simona Pilotto , Sagar Chittori , Sarah Picaud , Sara Marchese , Giuseppe Ciossani , Federico Forneris , Panagis Filippakopoulos , Guy Schoehn , Daniela Rhodes , Sriram Subramaniam , Andrea Mattevi Cell Reports 27, 387 - 399.e7 DOI: 10.1016/j.celrep.2019.03.061 Diamond Proposal Number(s): [16082] Open Access Show Abstract ▼ Abstract: LSD1 and LSD2 are homologous histone demethylases with opposite biological outcomes related to chromatin silencing and transcription elongation, respectively. Unlike LSD1, LSD2 nucleosome-demethylase activity relies on a specific linker peptide from the multidomain protein NPAC. We used single-particle cryoelectron microscopy (cryo-EM), in combination with kinetic and mutational analysis, to analyze the mechanisms underlying the function of the human LSD2/NPAC-linker/nucleosome complex. Weak interactions between LSD2 and DNA enable multiple binding modes for the association of the demethylase to the nucleosome. The demethylase thereby captures mono- and dimethyl Lys4 of the H3 tail to afford histone demethylation. Our studies also establish that the dehydrogenase domain of NPAC serves as a catalytically inert oligomerization module. While LSD1/CoREST forms a nucleosome docking platform at silenced gene promoters, LSD2/NPAC is a multifunctional enzyme complex with flexible linkers, tailored for rapid chromatin modification, in conjunction with the advance of the RNA polymerase on actively transcribed genes.	Apr 2019

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