Tat stimulates cotranscriptional capping of HIV mRNA.
TLDR
This work investigates how capping and methylation of HIV pre-mRNAs are coupled to Pol II elongation and implicates capping in an elongation checkpoint critical to HIV gene expression.About:
This article is published in Molecular Cell.The article was published on 2002-09-01 and is currently open access. It has received 131 citations till now. The article focuses on the topics: Capping enzyme & RNA polymerase II.read more
Citations
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Journal ArticleDOI
Coupling mRNA processing with transcription in time and space
TL;DR: Experiments using sophisticated new methods for analysis of nascent RNA have provided important insights into the relative amount of co- transcriptional and post-transcriptional processing, the relationship between mRNA elongation and processing, and the role of the Pol II carboxy-terminal domain (CTD) in regulating these processes.
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"Cotranscriptionality": the transcription elongation complex as a nexus for nuclear transactions
Roberto Perales,David Bentley +1 more
TL;DR: RNA maturation factors are not the only nuclear machines whose work is organized cotranscriptionally around the TEC scaffold, and TECs can be viewed as potent "community organizers" within the nucleus.
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RNA polymerase II pauses and associates with pre-mRNA processing factors at both ends of genes
TL;DR: Results suggest that promoters may help specify recruitment of 3′ end processing factors, and propose a dual-pausing model wherein elongation arrests near the transcription start site and in the 3′ flank to allow co-transcriptional processing by factors recruited to the pol II ternary complex.
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Promoter-proximal pausing of RNA polymerase II: a nexus of gene regulation
Leighton J. Core,Karen Adelman +1 more
TL;DR: In this review, Core et al. discuss the recent advances in understanding of the early steps in Pol II transcription, highlighting the events and factors involved in the establishment and release of paused Pol II.
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The multifactorial nature of HIV-1 latency
Kara G. Lassen,Yefei Han,Yan Zhou,Janet M. Siliciano,Robert F. Siliciano,Robert F. Siliciano +5 more
TL;DR: Latency might result from insufficient nuclear levels of the crucial activation-dependent host transcription factors required to overcome the transcriptional interference that is an automatic consequence of the nature of HIV-1 integration sites.
References
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A Novel CDK9-Associated C-Type Cyclin Interacts Directly with HIV-1 Tat and Mediates Its High-Affinity, Loop-Specific Binding to TAR RNA
Ping Wei,Mitchell E Garber,Mitchell E Garber,Shi-Min Fang,Wolfgang H. Fischer,Katherine A. Jones +5 more
TL;DR: It is proposed that Tat directs cyclin T-CDK9 to RNAPII through cooperative binding to TAR RNA, and confers a requirement for sequences in the loop of TAR that are not recognized by Tat alone.
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Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription
TL;DR: A dynamic association of mRNA processing factors with differently modified forms of the polymerase throughout the transcription cycle is suggested.
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P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II.
TL;DR: The fraction of initiating RNA polymerase II molecules that produce full-length transcripts is controlled by a selection process that occurs early in the elongation phase of the transcription cycle.
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5′-Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II
Susan McCracken,Nova Fong,Emanuel Rosonina,Krassimir Yankulov,David P. Siderovski,Andrew Hessel,Foster Stephen,Amgen Est Program,Stewart Shuman,David Bentley +9 more
TL;DR: Results suggest that Pol II-specific capping of nascent transcripts in vivo is enhanced by recruitment of the capping enzymes to the CTD and capping is co-ordinated with CTD phosphorylation.
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mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain
TL;DR: In vitro and in vivo evidence is provided that capping enzyme is recruited to the transcription complex via phosphorylation of the RNA polymerase CTD, which is blocked by the CTD-kinase inhibitor H8.