ArticleProceedings of the National Academy of Sciences of the United States of America2003
The initiation-elongation transition: lateral mobility of RNA in RNA polymerase II complexes is greatly reduced at +8/+9 and absent by +23.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- The molecular basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2026Review
- Plant organellar DNA primase-helicase synthesizes RNA primers for organellar DNA polymerases using a unique recognition sequence.Nucleic acids research · 2017Article
- PIC Activation through Functional Interplay between Mediator and TFIIH.Journal of molecular biology · 2017Article
- Single molecule microscopy reveals mechanistic insight into RNA polymerase II preinitiation complex assembly and transcriptional activity.Nucleic acids research · 2016Article
- Gdown1 Associates Efficiently with RNA Polymerase II after Promoter Clearance and Displaces TFIIF during Transcript Elongation.PloS one · 2016Article
- The fidelity of transcription: RPB1 (RPO21) mutations that increase transcriptional slippage in S. cerevisiae.The Journal of biological chemistry · 2013Article
- The Spt4-Spt5 complex: a multi-faceted regulator of transcription elongation.Biochimica et biophysica acta · 2013Review
- Promoter clearance by RNA polymerase II.Biochimica et biophysica acta · 2013Review
- Inactivated RNA polymerase II open complexes can be reactivated with TFIIE.The Journal of biological chemistry · 2012Article
- Transcription factor TFIIF is not required for initiation by RNA polymerase II, but it is essential to stabilize transcription factor TFIIB in early elongation complexes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Curaxins: anticancer compounds that simultaneously suppress NF-κB and activate p53 by targeting FACT.Science translational medicine · 2011Article
- The functions of TFIIF during initiation and transcript elongation are differentially affected by phosphorylation by casein kinase 2.The Journal of biological chemistry · 2011Article
- Single-molecule studies of RNA polymerase: one singular sensation, every little step it takes.Molecular cell · 2011Review
- Pol II waiting in the starting gates: Regulating the transition from transcription initiation into productive elongation.Biochimica et biophysica acta · 2011Review
- Rearrangement of the RNA polymerase subunit H and the lower jaw in archaeal elongation complexes.Nucleic acids research · 2010Article
- Transcription elongation complex stability: the topological lock.The Journal of biological chemistry · 2009Article
- TATA-binding protein and transcription factor IIB induce transcript slipping during early transcription by RNA polymerase II.The Journal of biological chemistry · 2009Article
- The structure of a transcribing T7 RNA polymerase in transition from initiation to elongation.Science (New York, N.Y.) · 2008Article
- Single-molecule tracking of mRNA exiting from RNA polymerase II.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- An 8 nt RNA triggers a rate-limiting shift of RNA polymerase II complexes into elongation.The EMBO journal · 2006Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
RNA polymerase II transcription complexes stalled shortly after initiation over a repetitive segment of the template can undergo efficient transcript slippage, during which the 3' end of the RNA slides upstream and then re-pairs with the template, allowing transcription to continue. In the present study, we have used transcript slippage as an assay to identify possible structural transitions that occur as the polymerase passes from the initiation to the elongation phase of transcription. We reasoned that transcript slippage would not occur in fully processive complexes. We constructed a series of templates that allowed us to stall RNA polymerase II after the synthesis of a repetitive sequence (5'-CUCUCU-3') at varying distances downstream of +1. We found that polymerase must synthesize at least a 23-nt RNA to attain resistance to transcript slippage. The ability to undergo slippage was lost in two discrete steps, suggestive of two distinct transitions. The first transition is the formation of the 8- to 9-bp mature RNA-DNA hybrid, when slippage abruptly dropped by 10-fold. However, easily detectable slippage continued until 14 more bonds were made. Thus, although the transcript becomes tightly constrained within the transcription complex once the hybrid reaches its final length, much more RNA synthesis is required before the RNA is no longer able to slip upstream along the template. This last point may reflect an important stabilizing role for the interaction of the polymerase with the transcript well upstream of the RNA-DNA hybrid.
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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.