ArticleNucleic acids research2008
Analysis of factor interactions with RNA polymerase II elongation complexes using a new electrophoretic mobility shift assay.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
36 citing papers in PubMed.
- Involvement of Human Cellular Proteins and Structures in Realization of the HIV Life Cycle: A Comprehensive Review, 2024.Viruses · 2024Review
- Enhancer RNAs stimulate Pol II pause release by harnessing multivalent interactions to NELF.Nature communications · 2022Article
- Simplicity is the Ultimate Sophistication-Crosstalk of Post-translational Modifications on the RNA Polymerase II.Journal of molecular biology · 2021Review
- Exploring histone loading on HIV DNA reveals a dynamic nucleosome positioning between unintegrated and integrated viral genome.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Promoter-proximal pausing mediated by the exon junction complex regulates splicing.Nature communications · 2019Article
- Article
- Structure of a transcribing RNA polymerase II-DSIF complex reveals a multidentate DNA-RNA clamp.Nature structural & molecular biology · 2017Article
- Identification of Regions in the Spt5 Subunit of DRB Sensitivity-inducing Factor (DSIF) That Are Involved in Promoter-proximal Pausing.The Journal of biological chemistry · 2017Article
- The yeast transcription elongation factor Spt4/5 is a sequence-specific RNA binding protein.Protein science : a publication of the Protein Society · 2016Article
- Biochemical Analysis of Yeast Suppressor of Ty 4/5 (Spt4/5) Reveals the Importance of Nucleic Acid Interactions in the Prevention of RNA Polymerase II Arrest.The Journal of biological chemistry · 2016Article
- Article
- Structures and Functions of the Multiple KOW Domains of Transcription Elongation Factor Spt5.Molecular and cellular biology · 2015Article
- Comparative Analysis of Tat-Dependent and Tat-Deficient Natural Lentiviruses.Veterinary sciences · 2015Review
- THZ1 Reveals Roles for Cdk7 in Co-transcriptional Capping and Pausing.Molecular cell · 2015Article
- Integrator complex regulates NELF-mediated RNA polymerase II pause/release and processivity at coding genes.Nature communications · 2014Article
- Enhancer RNA facilitates NELF release from immediate early genes.Molecular cell · 2014Article
- Negative elongation factor is required for the maintenance of proviral latency but does not induce promoter-proximal pausing of RNA polymerase II on the HIV long terminal repeat.Molecular and cellular biology · 2014Article
- Regulation of RNA polymerase II termination by phosphorylation of Gdown1.The Journal of biological chemistry · 2014Article
- Transcriptional control of HIV latency: cellular signaling pathways, epigenetics, happenstance and the hope for a cure.Virology · 2014Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The elongation phase of transcription by RNA polymerase II (RNAP II) is controlled by a carefully orchestrated series of interactions with both negative and positive factors. However, due to the limitations of current methods and techniques, not much is known about whether and how these proteins physically associate with the engaged polymerases. To gain insight into the detailed mechanisms involved, we established an experimental system for analyzing direct factor interactions to RNAP II elongation complexes on native gels, namely elongation complex electrophoretic mobility shift assay (EC-EMSA). This new assay effectively allowed detection of interactions of TFIIF, TTF2, TFIIS, DSIF and P-TEFb with elongation complexes generated from a natural promoter using an immobilized template. As an application of this assay system, we characterized the association of transcription elongation factor DSIF with RNAP II elongation complexes and discovered that the nascent transcript facilitated recruitment of DSIF. Examples of how the system can be manipulated to address different questions are provided. EC-EMSA should be useful for further investigation of factor interactions with RNAP II elongation complexes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.