ORCID Profile
0000-0003-4964-6147
Current Organisations
Aarhus University
,
IT University of Copenhagen
,
University College London
,
Imperial College London
,
Københavns Universitet
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Publications
Interacting partners of the Tfb2 subunit from yeast TFIIH
Publisher: Elsevier BV
Date: 2010
DOI: 10.1016/J.DNAREP.2009.10.002
Abstract: TFIIH is an evolutionary conserved eukaryotic multi-protein complex composed of ten subunits. It is involved in transcription, cell cycle regulation, RNA splicing and the nucleotide excision DNA repair pathway (NER). Depending on the process in which it is functioning, the composition of TFIIH varies and activities of its subunits are differentially regulated. Here we focused on interplay between the Ssl2, Tfb2 and Tfb5 subunits of TFIIH from Saccharomyces cerevisiae. We found that Tfb2 bridges the Ssl2 helicase and the NER-specific Tfb5 subunit. Moreover, the Tfb5-interacting domain of Tfb2 also binds nucleic acids (NA), although the addition of Tfb5 triggers dissociation of NA from Tfb2. In yeast cells, deletion of TFB5 is more detrimental to NER than loss of the Tfb5/NA-interacting domain of Tfb2, while combining these mutations resulted in suppression of the UV sensitivity of tfb5Delta. The implications of our findings in regards to TFIIH function and group A trichothiodystrophy, an inherited disease associated with mutations in the human TFB5 gene, are discussed.
CDK13 cooperates with CDK12 to control global RNA polymerase II processivity
Publisher: American Association for the Advancement of Science (AAAS)
Date: 05-2020
Abstract: CDK12 and CDK13 regulate POLII elongation rate and processivity and influence the selection of transcription termination sites.
Developmental regulation of neuronal gene expression by Elongator complex protein 1 dosage
Publisher: Elsevier BV
Date: 07-2022
Transcript Elongation by RNA Polymerase II
Publisher: Annual Reviews
Date: 07-06-2010
DOI: 10.1146/ANNUREV.BIOCHEM.78.062807.091425
Abstract: Until recently, it was generally assumed that essentially all regulation of transcription takes place via regions adjacent to the coding region of a gene—namely promoters and enhancers—and that, after recruitment to the promoter, the polymerase simply behaves like a machine, quickly “reading the gene.” However, over the past decade a revolution in this thinking has occurred, culminating in the idea that transcript elongation is extremely complex and highly regulated and, moreover, that this process significantly affects both the organization and integrity of the genome. This review addresses basic aspects of transcript elongation by RNA polymerase II (RNAPII) and how it relates to other DNA-related processes.
An Rtt109-Independent Role for Vps75 in Transcription-Associated Nucleosome Dynamics
Publisher: Informa UK Limited
Date: 08-2009
DOI: 10.1128/MCB.01882-08
Vps75, A New Yeast Member of the NAP Histone Chaperone Family
Publisher: Elsevier BV
Date: 04-2007
An Iron-Sulfur Cluster Domain in Elp3 Important for the Structural Integrity of Elongator
Publisher: Elsevier BV
Date: 2009
Studying RNA–Protein Interactions In Vivo By RNA Immunoprecipitation
Publisher: Humana Press
Date: 2011
DOI: 10.1007/978-1-61779-316-5_19
Abstract: The crucial roles played by RNA-binding proteins in all aspects of RNA metabolism, particularly in the regulation of transcription, have become increasingly evident. Moreover, other factors that do not directly interact with RNA molecules can nevertheless function proximally to RNA polymerases and have significant effects on gene expression. RNA immunoprecipitation (RIP) is a powerful technique used to detect direct and indirect interactions between in idual proteins and specific RNA molecules in vivo. Here, we describe RIP methods for both yeast and mammalian cells.
RNA Immunoprecipitation to Determine RNA-Protein Associations In Vivo
Publisher: Cold Spring Harbor Laboratory
Date: 06-2009
DOI: 10.1101/PDB.PROT5234
Abstract: The crucial roles of RNA-binding proteins in all aspects of RNA metabolism, particularly in the regulation of mRNAs and subsequent control of gene expression patterns, have become increasingly evident. RNA immunoprecipitation (RIP) is a powerful technique used to detect the association of in idual proteins with specific RNA molecules in vivo. Live cells are treated with formaldehyde to generate protein-RNA cross-links between proximal molecules. Following immunoprecipitation of a protein of interest and cross-link reversal, associated RNAs can be recovered, characterized, and quantitated by reverse transcriptase polymerase chain reaction (RT-PCR). Protein association with specific RNA regions can be performed under a variety of conditions (e.g., different environmental and cell-cycle states) and/or in mutant strains. Furthermore, because formaldehyde inactivates cellular enzymes essentially immediately upon addition to cells, RIP provides snapshots of protein-RNA interactions at specific time points and hence is useful for kinetic analyses of events occurring on RNA in vivo. The basics of RIP are very similar to chromatin immunoprecipitation (ChIP), but with some caveats that are important to appreciate to take full advantage of the possibilities afforded by RIP.
Related Organisations
The Francis Crick Institute
Location: United Kingdom of Great Britain and Northern Ireland
Cancer Research UK
Location: United Kingdom of Great Britain and Northern Ireland
University College London
Location: United Kingdom of Great Britain and Northern Ireland
Stanford University School Of Medicine
Location: United States of America
Imperial College London
Location: United Kingdom of Great Britain and Northern Ireland
Related Funding Activities
No related grants have been discovered for Jesper Svejstrup.