Cramer, Patrick

[["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.contributor.author","Kabinger, Florian"],["dc.contributor.author","Stiller, Carina"],["dc.contributor.author","Schmitzová, Jana"],["dc.contributor.author","Dienemann, C."],["dc.contributor.author","Kokic, Goran"],["dc.contributor.author","Hillen, Hauke S."],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Cramer, Patrick"],["dc.date.accessioned","2021-09-01T06:42:22Z"],["dc.date.available","2021-09-01T06:42:22Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract Molnupiravir is an orally available antiviral drug candidate currently in phase III trials for the treatment of patients with COVID-19. Molnupiravir increases the frequency of viral RNA mutations and impairs SARS-CoV-2 replication in animal models and in humans. Here, we establish the molecular mechanisms underlying molnupiravir-induced RNA mutagenesis by the viral RNA-dependent RNA polymerase (RdRp). Biochemical assays show that the RdRp uses the active form of molnupiravir, β- d - N 4 -hydroxycytidine (NHC) triphosphate, as a substrate instead of cytidine triphosphate or uridine triphosphate. When the RdRp uses the resulting RNA as a template, NHC directs incorporation of either G or A, leading to mutated RNA products. Structural analysis of RdRp–RNA complexes that contain mutagenesis products shows that NHC can form stable base pairs with either G or A in the RdRp active center, explaining how the polymerase escapes proofreading and synthesizes mutated RNA. This two-step mutagenesis mechanism probably applies to various viral polymerases and can explain the broad-spectrum antiviral activity of molnupiravir."],["dc.identifier.doi","10.1038/s41594-021-00651-0"],["dc.identifier.pii","651"],["dc.identifier.pmid","34381216"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89038"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/381"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/171"],["dc.identifier.url","https://for2848.gwdguser.de/literature/publications/28"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-455"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","FOR 2848: Architektur und Heterogenität der inneren mitochondrialen Membran auf der Nanoskala"],["dc.relation","FOR 2848 | St01: Structure and distribution of ribosomes at the inner mitochondrial membrane"],["dc.relation.eissn","1545-9985"],["dc.relation.issn","1545-9993"],["dc.relation.workinggroup","RG Cramer"],["dc.relation.workinggroup","RG Hillen (Structure and Function of Molecular Machines)"],["dc.rights","CC BY 4.0"],["dc.title","Mechanism of molnupiravir-induced SARS-CoV-2 mutagenesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e71533"],["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Xiong, Le"],["dc.contributor.author","Tolen, Erik A."],["dc.contributor.author","Choi, Jinmi"],["dc.contributor.author","Velychko, Sergiy"],["dc.contributor.author","Caizzi, Livia"],["dc.contributor.author","Velychko, Taras"],["dc.contributor.author","Adachi, Kenjiro"],["dc.contributor.author","MacCarthy, Caitlin M."],["dc.contributor.author","Lidschreiber, Michael"],["dc.contributor.author","Cramer, Patrick"],["dc.contributor.author","Schöler, Hans R."],["dc.date.accessioned","2022-06-01T09:40:03Z"],["dc.date.available","2022-06-01T09:40:03Z"],["dc.date.issued","2022"],["dc.description.abstract","The transcription factor Oct4 is essential for the maintenance and induction of stem cell pluripotency, but its functional roles are not fully understood. Here, we investigate the functions of Oct4 by depleting and subsequently recovering it in mouse embryonic stem cells (ESCs) and conducting a time-resolved multiomics analysis. Oct4 depletion leads to an immediate loss of its binding to enhancers, accompanied by a decrease in mRNA synthesis from its target genes that are part of the transcriptional network that maintains pluripotency. Gradual decrease of Oct4 binding to enhancers does not immediately change the chromatin accessibility but reduces transcription of enhancers. Conversely, partial recovery of Oct4 expression results in a rapid increase in chromatin accessibility, whereas enhancer transcription does not fully recover. These results indicate different concentration-dependent activities of Oct4. Whereas normal ESC levels of Oct4 are required for transcription of pluripotency enhancers, low levels of Oct4 are sufficient to retain chromatin accessibility, likely together with other factors such as Sox2."],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft"],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft"],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft"],["dc.description.sponsorship"," European Research Council"],["dc.description.sponsorship","Max Planck Institute for Multidisciplinary Sciences"],["dc.description.sponsorship"," European Research Council"],["dc.description.sponsorship"," Max Planck Society"],["dc.description.sponsorship","Max Planck Institute for Molecular Biomedicine"],["dc.identifier.doi","10.7554/eLife.71533"],["dc.identifier.pmid","35621159"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/108626"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/506"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-572"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","2050-084X"],["dc.relation.workinggroup","RG Cramer"],["dc.rights","CC BY 4.0"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Oct4 differentially regulates chromatin opening and enhancer transcription in pluripotent stem cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e9873"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular Systems Biology"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Lidschreiber, Katja"],["dc.contributor.author","Jung, Lisa A"],["dc.contributor.author","von der Emde, Henrik"],["dc.contributor.author","Dave, Kashyap"],["dc.contributor.author","Taipale, Jussi"],["dc.contributor.author","Cramer, Patrick"],["dc.contributor.author","Lidschreiber, Michael"],["dc.date.accessioned","2022-02-21T16:27:49Z"],["dc.date.available","2022-02-21T16:27:49Z"],["dc.date.issued","2021"],["dc.description.abstract","The growth of human cancer cells is driven by aberrant enhancer and gene transcription activity. Here, we use transient transcriptome sequencing (TT-seq) to map thousands of transcriptionally active putative enhancers in fourteen human cancer cell lines covering seven types of cancer. These enhancers were associated with cell type-specific gene expression, enriched for genetic variants that predispose to cancer, and included functionally verified enhancers. Enhancer-promoter (E-P) pairing by correlation of transcription activity revealed ~ 40,000 putative E-P pairs, which were depleted for housekeeping genes and enriched for transcription factors, cancer-associated genes, and 3D conformational proximity. The cell type specificity and transcription activity of target genes increased with the number of paired putative enhancers. Our results represent a rich resource for future studies of gene regulation by enhancers and their role in driving cancerous cell growth."],["dc.identifier.doi","10.15252/msb.20209873"],["dc.identifier.pmid","33502116"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100157"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/217"],["dc.language.iso","en"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.issn","1744-4292"],["dc.relation.workinggroup","RG Cramer"],["dc.rights","CC BY 4.0"],["dc.title","Transcriptionally active enhancers in human cancer cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e107015"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Sawicka, Anna"],["dc.contributor.author","Villamil, Gabriel"],["dc.contributor.author","Lidschreiber, Michael"],["dc.contributor.author","Darzacq, Xavier"],["dc.contributor.author","Dugast-Darzacq, Claire"],["dc.contributor.author","Schwalb, Björn"],["dc.contributor.author","Cramer, Patrick"],["dc.date.accessioned","2022-02-21T16:28:07Z"],["dc.date.available","2022-02-21T16:28:07Z"],["dc.date.issued","2021"],["dc.description.abstract","Eukaryotic RNA polymerase II (Pol II) contains a tail-like, intrinsically disordered carboxy-terminal domain (CTD) comprised of heptad-repeats, that functions in coordination of the transcription cycle and in coupling transcription to co-transcriptional processes. The CTD repeat number varies between species and generally increases with genome size, but the reasons for this are unclear. Here, we show that shortening the CTD in human cells to half of its length does not generally change pre-mRNA synthesis or processing in cells. However, CTD shortening decreases the duration of promoter-proximal Pol II pausing, alters transcription of putative enhancer elements, and delays transcription activation after stimulation of the MAP kinase pathway. We suggest that a long CTD is required for efficient enhancer-dependent recruitment of Pol II to target genes for their rapid activation."],["dc.identifier.doi","10.15252/embj.2020107015"],["dc.identifier.pmid","33555055"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100160"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/229"],["dc.language.iso","en"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.relation.workinggroup","RG Cramer"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","Transcription activation depends on the length of the RNA polymerase II C-terminal domain"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Nature"],["dc.contributor.author","Kokic, Goran"],["dc.contributor.author","Wagner, Felix R."],["dc.contributor.author","Chernev, Aleksandar"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Cramer, Patrick"],["dc.date.accessioned","2021-10-01T09:57:44Z"],["dc.date.available","2021-10-01T09:57:44Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract Transcription-coupled DNA repair removes bulky DNA lesions from the genome 1,2 and protects cells against ultraviolet (UV) irradiation 3 . Transcription-coupled DNA repair begins when RNA polymerase II (Pol II) stalls at a DNA lesion and recruits the Cockayne syndrome protein CSB, the E3 ubiquitin ligase, CRL4 CSA and UV-stimulated scaffold protein A (UVSSA) 3 . Here we provide five high-resolution structures of Pol II transcription complexes containing human transcription-coupled DNA repair factors and the elongation factors PAF1 complex (PAF) and SPT6. Together with biochemical and published 3,4 data, the structures provide a model for transcription–repair coupling. Stalling of Pol II at a DNA lesion triggers replacement of the elongation factor DSIF by CSB, which binds to PAF and moves upstream DNA to SPT6. The resulting elongation complex, EC TCR , uses the CSA-stimulated translocase activity of CSB to pull on upstream DNA and push Pol II forward. If the lesion cannot be bypassed, CRL4 CSA spans over the Pol II clamp and ubiquitylates the RPB1 residue K1268, enabling recruitment of TFIIH to UVSSA and DNA repair. Conformational changes in CRL4 CSA lead to ubiquitylation of CSB and to release of transcription-coupled DNA repair factors before transcription may continue over repaired DNA."],["dc.identifier.doi","10.1038/s41586-021-03906-4"],["dc.identifier.pii","3906"],["dc.identifier.pmid","34526721"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89904"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/340"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-469"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1476-4687"],["dc.relation.issn","0028-0836"],["dc.relation.workinggroup","RG Cramer"],["dc.rights","CC BY 4.0"],["dc.title","Structural basis of human transcription–DNA repair coupling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","493"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","501"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Dombrowski, Marco"],["dc.contributor.author","Engeholm, Maik"],["dc.contributor.author","Dienemann, Christian"],["dc.contributor.author","Dodonova, Svetlana"],["dc.contributor.author","Cramer, Patrick"],["dc.date.accessioned","2022-06-01T09:39:10Z"],["dc.date.available","2022-06-01T09:39:10Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract Throughout the genome, nucleosomes often form regular arrays that differ in nucleosome repeat length (NRL), occupancy of linker histone H1 and transcriptional activity. Here, we report cryo-EM structures of human H1-containing tetranucleosome arrays with four physiologically relevant NRLs. The structures show a zig-zag arrangement of nucleosomes, with nucleosomes 1 and 3 forming a stack. H1 binding to stacked nucleosomes depends on the NRL, whereas H1 always binds to the non-stacked nucleosomes 2 and 4. Short NRLs lead to altered trajectories of linker DNA, and these altered trajectories sterically impair H1 binding to the stacked nucleosomes in our structures. As the NRL increases, linker DNA trajectories relax, enabling H1 contacts and binding. Our results provide an explanation for why arrays with short NRLs are depleted of H1 and suited for transcription, whereas arrays with long NRLs show full H1 occupancy and can form transcriptionally silent heterochromatin regions."],["dc.identifier.doi","10.1038/s41594-022-00768-w"],["dc.identifier.pii","768"],["dc.identifier.pmid","35581345"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/108404"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/531"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-572"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1545-9985"],["dc.relation.issn","1545-9993"],["dc.relation.workinggroup","RG Cramer"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Histone H1 binding to nucleosome arrays depends on linker DNA length and trajectory"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","726"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Systems Biology"],["dc.bibliographiccitation.lastpage","15"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Eser, Philipp"],["dc.contributor.author","Demel, Carina"],["dc.contributor.author","Maier, Kerstin C"],["dc.contributor.author","Schwalb, Björn"],["dc.contributor.author","Pirkl, Nicole"],["dc.contributor.author","Martin, Dietmar E"],["dc.contributor.author","Cramer, Patrick"],["dc.contributor.author","Tresch, Achim"],["dc.date.accessioned","2022-03-01T11:46:28Z"],["dc.date.available","2022-03-01T11:46:28Z"],["dc.date.issued","2014"],["dc.description.abstract","During the cell cycle, the levels of hundreds of mRNAs change in a periodic manner, but how this is achieved by alterations in the rates of mRNA synthesis and degradation has not been studied systematically. Here, we used metabolic RNA labeling and comparative dynamic transcriptome analysis (cDTA) to derive mRNA synthesis and degradation rates every 5 min during three cell cycle periods of the yeast Saccharomyces cerevisiae. A novel statistical model identified 479 genes that show periodic changes in mRNA synthesis and generally also periodic changes in their mRNA degradation rates. Peaks of mRNA degradation generally follow peaks of mRNA synthesis, resulting in sharp and high peaks of mRNA levels at defined times during the cell cycle. Whereas the timing of mRNA synthesis is set by upstream DNA motifs and their associated transcription factors (TFs), the synthesis rate of a periodically expressed gene is apparently set by its core promoter."],["dc.identifier.doi","10.1002/msb.20140001"],["dc.identifier.gro","3142211"],["dc.identifier.isi","000333904100002"],["dc.identifier.pmid","24489117"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14452"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103682"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1744-4292"],["dc.relation.issn","1744-4292"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","Periodic mRNA synthesis and degradation co‐operate during cell cycle gene expression"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","382"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Nature Structural & Molecular Biology"],["dc.bibliographiccitation.lastpage","387"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Farnung, Lucas"],["dc.contributor.author","Ochmann, Moritz"],["dc.contributor.author","Engeholm, Maik"],["dc.contributor.author","Cramer, Patrick"],["dc.date.accessioned","2022-02-22T12:16:36Z"],["dc.date.available","2022-02-22T12:16:36Z"],["dc.date.issued","2021"],["dc.description.abstract","Efficient transcription of RNA polymerase II (Pol II) through nucleosomes requires the help of various factors. Here we show biochemically that Pol II transcription through a nucleosome is facilitated by the chromatin remodeler Chd1 and the histone chaperone FACT when the elongation factors Spt4/5 and TFIIS are present. We report cryo-EM structures of transcribing Saccharomyces cerevisiae Pol II-Spt4/5-nucleosome complexes with bound Chd1 or FACT. In the first structure, Pol II transcription exposes the proximal histone H2A-H2B dimer that is bound by Spt5. Pol II has also released the inhibitory DNA-binding region of Chd1 that is poised to pump DNA toward Pol II. In the second structure, Pol II has generated a partially unraveled nucleosome that binds FACT, which excludes Chd1 and Spt5. These results suggest that Pol II progression through a nucleosome activates Chd1, enables FACT binding and eventually triggers transfer of FACT together with histones to upstream DNA."],["dc.identifier.doi","10.1038/s41594-021-00578-6"],["dc.identifier.pmid","33846633"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100171"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/267"],["dc.language.iso","en"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1545-9985"],["dc.relation.issn","1545-9993"],["dc.relation.workinggroup","RG Cramer"],["dc.rights","CC BY 4.0"],["dc.title","Structural basis of nucleosome transcription mediated by Chd1 and FACT"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Communications Biology"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Fianu, Isaac"],["dc.contributor.author","Dienemann, Christian"],["dc.contributor.author","Aibara, Shintaro"],["dc.contributor.author","Schilbach, Sandra"],["dc.contributor.author","Cramer, Patrick"],["dc.date.accessioned","2022-02-22T07:46:36Z"],["dc.date.available","2022-02-22T07:46:36Z"],["dc.date.issued","2021"],["dc.description.abstract","Nuclear import of RNA polymerase II (Pol II) involves the conserved factor RPAP2. Here we report the cryo-electron microscopy (cryo-EM) structure of mammalian Pol II in complex with human RPAP2 at 2.8 Å resolution. The structure shows that RPAP2 binds between the jaw domains of the polymerase subunits RPB1 and RPB5. RPAP2 is incompatible with binding of downstream DNA during transcription and is displaced upon formation of a transcription pre-initiation complex."],["dc.identifier.doi","10.1038/s42003-021-02088-z"],["dc.identifier.pmid","34021257"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100168"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/260"],["dc.language.iso","en"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.issn","2399-3642"],["dc.relation.orgunit","Max-Planck-Institut für biophysikalische Chemie"],["dc.relation.workinggroup","RG Cramer"],["dc.rights","CC BY 4.0"],["dc.title","Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1013.e11"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","1026.e11"],["dc.bibliographiccitation.volume","81"],["dc.contributor.author","Rawat, Prashant"],["dc.contributor.author","Boehning, Marc"],["dc.contributor.author","Hummel, Barbara"],["dc.contributor.author","Aprile-Garcia, Fernando"],["dc.contributor.author","Pandit, Anwit S."],["dc.contributor.author","Eisenhardt, Nathalie"],["dc.contributor.author","Khavaran, Ashkan"],["dc.contributor.author","Niskanen, Einari"],["dc.contributor.author","Vos, Seychelle M."],["dc.contributor.author","Palvimo, Jorma J."],["dc.contributor.author","Pichler, Andrea"],["dc.contributor.author","Cramer, Patrick"],["dc.contributor.author","Sawarkar, Ritwick"],["dc.date.accessioned","2022-02-21T16:27:54Z"],["dc.date.available","2022-02-21T16:27:54Z"],["dc.date.issued","2021"],["dc.description.abstract","In response to stress, human cells coordinately downregulate transcription and translation of housekeeping genes. To downregulate transcription, the negative elongation factor (NELF) is recruited to gene promoters impairing RNA polymerase II elongation. Here we report that NELF rapidly forms nuclear condensates upon stress in human cells. Condensate formation requires NELF dephosphorylation and SUMOylation induced by stress. The intrinsically disordered region (IDR) in NELFA is necessary for nuclear NELF condensation and can be functionally replaced by the IDR of FUS or EWSR1 protein. We find that biomolecular condensation facilitates enhanced recruitment of NELF to promoters upon stress to drive transcriptional downregulation. Importantly, NELF condensation is required for cellular viability under stressful conditions. We propose that stress-induced NELF condensates reported here are nuclear counterparts of cytosolic stress granules. These two stress-inducible condensates may drive the coordinated downregulation of transcription and translation, likely forming a critical node of the stress survival strategy."],["dc.identifier.doi","10.1016/j.molcel.2021.01.016"],["dc.identifier.pmid","33548202"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100158"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/221"],["dc.language.iso","en"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1097-4164"],["dc.relation.issn","1097-2765"],["dc.relation.workinggroup","RG Cramer"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","Stress-induced nuclear condensation of NELF drives transcriptional downregulation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]