The RNA cleavage activity of RNA polymerase III is mediated by an essential TFIIS-like subunit and is important for transcription termination

Chédin, Stéphane; Riva, Michel; Schultz, Patrick; Sentenac, André; Carles, Christophe

doi:10.1101/gad.12.24.3857

Cited by 162 publications

(249 citation statements)

References 80 publications

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“…Landrieux et al (2006) showed that C11 RNA cleavage activity is not required for correct recognition of the RNAPIII terminator elements and release of the newly synthesized transcript. However, C11 itself, but not its cleavage activity, is required for reinitiation (Chedin et al 1998;Landrieux et al 2006). These experiments strongly suggest that termination and cleavage of the RNA precursor are not coupled in the RNAPIII transcription process.…”

Section: Rnapiii: a Terminator On Its Own?mentioning

confidence: 56%

“…5). C11 is an essential subunit that mediates the intrinsic RNA cleavage activity of RNAPIII (Whitehall et al 1994) and shows homology with the RNAPII subunit Rpb9 and to RNAPII elongation factor TFIIS (Chedin et al 1998). Landrieux et al (2006) showed that C11 RNA cleavage activity is not required for correct recognition of the RNAPIII terminator elements and release of the newly synthesized transcript.…”

Section: Rnapiii: a Terminator On Its Own?mentioning

confidence: 99%

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Transcription termination by nuclear RNA polymerases

Richard

Manley²

2009

Genes Dev.

289

326

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Gene transcription in the cell nucleus is a complex and highly regulated process. Transcription in eukaryotes requires three distinct RNA polymerases, each of which employs its own mechanisms for initiation, elongation, and termination. Termination mechanisms vary considerably, ranging from relatively simple to exceptionally complex. In this review, we describe the present state of knowledge on how each of the three RNA polymerases terminates and how mechanisms are conserved, or vary, from yeast to human.

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Section: Rnapiii: a Terminator On Its Own?mentioning

confidence: 56%

Section: Rnapiii: a Terminator On Its Own?mentioning

confidence: 99%

Transcription termination by nuclear RNA polymerases

Richard

Manley²

2009

Genes Dev.

289

326

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“…Curiously, the homologous subunit in RNA polymerase III, C11, also is essential for the intrinsic cleavage reaction carried out by that polymerase (74). However, there is no TFIIS-like cofactor required to stimulate cleavage for RNA polymerase III.…”

Section: Discussionmentioning

confidence: 99%

Intrinsic Transcript Cleavage in Yeast RNA Polymerase II Elongation Complexes

Weilbaecher

Awrey

Edwards

et al. 2003

Journal of Biological Chemistry

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Transcript elongation can be interrupted by a variety of obstacles, including certain DNA sequences, DNAbinding proteins, chromatin, and DNA lesions. Bypass of many of these impediments is facilitated by elongation factor TFIIS through a mechanism that involves cleavage of the nascent transcript by the RNA polymerase II/TFIIS elongation complex. Highly purified yeast RNA polymerase II is able to perform transcript hydrolysis in the absence of TFIIS. The "intrinsic" cleavage activity is greatly stimulated at mildly basic pH and requires divalent cations. Both arrested and stalled complexes can carry out the intrinsic cleavage reaction, although not all stalled complexes are equally efficient at this reaction. Arrested complexes in which the nascent transcript was cleaved in the absence of TFIIS were reactivated to readthrough blocks to elongation. Thus, cleavage of the nascent transcript is sufficient for reactivating some arrested complexes. Small RNA products released following transcript cleavage in stalled ternary complexes differ depending upon whether the cleavage has been induced by TFIIS or has occurred in mildly alkaline conditions. In contrast, both intrinsic and TFIIS-induced small RNA cleavage products are very similar when produced from an arrested ternary complex. Although ␣-amanitin interferes with the transcript cleavage stimulated by TFIIS, it has little effect on the intrinsic cleavage reaction. A mutant RNA polymerase previously shown to be refractory to TFIIS-induced transcript cleavage is essentially identical to the wild type polymerase in all tested aspects of intrinsic cleavage.Gene expression can be controlled by regulating any step of the transcription cycle: promoter binding, initiation, promoter escape, elongation, or termination. After transcript synthesis begins, the ability to suppress or complete the synthesis of an RNA transcript is vital to the cell, and a substantial and growing number of genes have been reported to be regulated during transcript elongation (1).The ternary elongation complex consists of the RNA polymerase, the template DNA, and the nascent RNA transcript. Surratt et al. (2) discovered that bacterial RNA polymerase ternary complexes have a mechanism for transcript shortening, endonucleolytic cleavage near the 3Ј-end of the transcript. After transcript cleavage, the 3Ј-fragment is released while the 5Ј-fragment is retained in an active ternary complex. A single cleavage event can liberate from 1 to 17 nt 1 of RNA bearing a 5Ј-monophosphate (3-6). Remarkably, transcription accurately resumes from the site of transcript cleavage to re-synthesize the excised RNA.Transcript cleavage activity is conserved in many DNA-dependent RNA polymerases, including bacterial RNA polymerases, vaccinia virus RNA polymerase (7), RNA polymerase I (8, 9), RNA polymerase II (10 -14), and RNA polymerase III (15). Accessory factors that stimulate transcript cleavage in ternary complexes have been identified in both prokaryotes (GreA and GreB) and eukaryotes (reviewed in Refs. 3,9,[16][17]...

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“…RNA cleavage leads to a new 3 0 -OH group at the RNA end at the polymerase active site, allowing RNA synthesis to resume [67][68][69]. RNAPs I and III possess a strong intrinsic RNA cleavage activity [70,71 ]. In RNAP III, cleavage activity is so strong that misincorporation cannot be detected unless a cleavagedeficient isoform of the enzyme is used [40 ].…”

Section: Error Removal: Rnap Backtracking and Rna Cleavagementioning

confidence: 99%

RNA polymerase fidelity and transcriptional proofreading

Sydow

Cramer

2009

Current Opinion in Structural Biology

144

133

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Whereas mechanisms underlying the fidelity of DNA polymerases (DNAPs) have been investigated in detail, RNA polymerase (RNAP) fidelity mechanisms remained poorly understood. New functional and structural studies now suggest how RNAPs select the correct nucleoside triphosphate (NTP) substrate to prevent transcription errors, and how the enzymes detect and remove a misincorporated nucleotide during proofreading. Proofreading begins with fraying of the misincorporated nucleotide away from the DNA template, which pauses transcription. Subsequent backtracking of RNAP by one position enables nucleolytic cleavage of an RNA dinucleotide that contains the misincorporated nucleotide. Since cleavage occurs at the same active site that is used for polymerization, the RNAP proofreading mechanism differs from that used by DNAPs, which contain a distinct nuclease specific active site.

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The RNA cleavage activity of RNA polymerase III is mediated by an essential TFIIS-like subunit and is important for transcription termination

Cited by 162 publications

References 80 publications

Transcription termination by nuclear RNA polymerases

Transcription termination by nuclear RNA polymerases

Intrinsic Transcript Cleavage in Yeast RNA Polymerase II Elongation Complexes

RNA polymerase fidelity and transcriptional proofreading

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