ArticleProceedings of the National Academy of Sciences of the United States of America1994
Molecular cloning of an essential subunit of RNA polymerase II elongation factor SIII.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 68 citations in OpenAlex.
- Structure of the transcribing RNA polymerase II-Elongin complex.Nature structural & molecular biology · 2023Article
- Cockayne syndrome B protein regulates recruitment of the Elongin A ubiquitin ligase to sites of DNA damage.The Journal of biological chemistry · 2017Article
- The structure and regulation of Cullin 2 based E3 ubiquitin ligases and their biological functions.Cell division · 2016Review
- Assembly of the Elongin A Ubiquitin Ligase Is Regulated by Genotoxic and Other Stresses.The Journal of biological chemistry · 2015Article
- Transcriptional properties of mammalian elongin A and its role in stress response.The Journal of biological chemistry · 2013Article
- The Role of Elongin BC-Containing Ubiquitin Ligases.Frontiers in oncology · 2012Article
- Mammalian Elongin A complex mediates DNA-damage-induced ubiquitylation and degradation of Rpb1.The EMBO journal · 2008Article
- In vivo requirement of the RNA polymerase II elongation factor elongin A for proper gene expression and development.Molecular and cellular biology · 2004Article
- dELL is an essential RNA polymerase II elongation factor with a general role in development.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Drosophila ELL is associated with actively elongating RNA polymerase II on transcriptionally active sites in vivo.The EMBO journal · 2001Article
- Transcriptional pause, arrest and termination sites for RNA polymerase II in mammalian N- and c-myc genes.Nucleic acids research · 1999Article
- The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families.Genes & development · 1998Article
- Fidelity of RNA polymerase II transcription controlled by elongation factor TFIIS.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- The inducible elongin A elongation activation domain: structure, function and interaction with the elongin BC complex.The EMBO journal · 1996Article
- Article
- Transcription syndromes and the role of RNA polymerase II general transcription factors in human disease.The Journal of clinical investigation · 1996Review
- Nuclear/cytoplasmic localization of the von Hippel-Lindau tumor suppressor gene product is determined by cell density.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Control of rRNA transcription in Escherichia coli.Microbiological reviews · 1995Review
- Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
A transcription factor designated SIII was recently purified from mammalian cells and shown to regulate the activity of the RNA polymerase II elongation complex. SIII is a heterotrimer composed of approximately 110-, 18-, and 15-kDa polypeptides and is capable of increasing the overall rate of RNA chain elongation by RNA polymerase II by suppressing transient pausing of polymerase at multiple sites on the DNA template. Here we describe the molecular cloning and characterization of a cDNA encoding the functional 15-kDa subunit (p15) of SIII. The p15 cDNA encodes a 112-amino-acid polypeptide with a calculated molecular mass of 12,473 Da and an electrophoretic mobility indistinguishable from that of the natural p15 subunit. When combined with the 110- and 18-kDa SIII subunits, bacterially expressed p15 efficiently replaces the natural p15 subunit in reconstitution of transcriptionally active SIII. A homology search revealed that the amino-terminal half of the SIII p15 subunit shares significant sequence similarity with a portion of the RNA-binding domain of Escherichia coli transcription termination protein rho and with the E. coli NusB protein, suggesting that SIII may be evolutionarily related to proteins involved in the control of transcription elongation in eubacteria.
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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.