Specific interaction of the murine transcription termination factor TTF I with class-I RNA polymerases

Kuhn, Anne; Bartsch, Ingrid; Grummt, Ingrid

doi:10.1038/344559a0

Cited by 102 publications

(106 citation statements)

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“…The differences might suggest different locations of the active sites of DNA and RNA polymerases from the point of arrest or from the point of contact between these enzymes and the terminator protein-replication terminus complex. The observation that the Reb1 protein of yeast while arresting RNAP I of yeast was incapable of arresting either T7 RNAP or DnaB helicase, as reported here, would suggest that the eukaryotic transcription terminator protein probably also interacts with the RNAPs that it arrests (40).…”

Section: Discussionmentioning

confidence: 82%

“…conjugational transfer, and DNA repair (11,12,19,31). RNAPs of yeast and mammalian cells are blocked by transcription terminator proteins that bind to specific DNA sequences (33,40). We were curious to test the specificity of blocks mediated by the yeast Reb1 protein since the topic is relevant to the possible mechanism of polar arrest of DNA and RNA chain elongation.…”

Section: Fate Of Tus Protein When Rnap Invades Tus-ter () Complex Fromentioning

confidence: 99%

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Mechanistic Studies on the Impact of Transcription on Sequence-specific Termination of DNA Replication and Vice Versa

Mohanty

Sahoo

Bastia

1998

Journal of Biological Chemistry

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Since DNA replication and transcription often temporally and spatially overlap each other, the impact of one process on the other is of considerable interest. We have reported previously that transcription is impeded at the replication termini of Escherichia coli and Bacillus subtilis in a polar mode and that, when transcription is allowed to invade a replication terminus from the permissive direction, arrest of replication fork at the terminus is abrogated. In the present report, we have addressed four significant questions pertaining to the mechanism of transcription impedance by the replication terminator proteins. Is transcription arrested at the replication terminus or does RNA polymerase dissociate from the DNA causing authentic transcription termination? How does transcription cause abrogation of replication fork arrest at the terminus? Are the points of arrest of the replication fork and transcription the same or are these different? Are eukaryotic RNA polymerases also arrested at prokaryotic replication termini? Our results show that replication terminator proteins of E. coli and B. subtilis arrest but do not terminate transcription. Passage of an RNA transcript through the replication terminus causes the dissociation of the terminator protein from the terminus DNA, thus causing abrogation of replication fork arrest. DNA and RNA chain elongation are arrested at different locations on the terminator sites. Finally, although bacterial replication terminator proteins blocked yeast RNA polymerases in a polar fashion, a yeast transcription terminator protein (Reb1p) was unable to block T7 RNA polymerase and E. coli DnaB helicase.The chromosomes of Escherichia coli and Bacillus subtilis, and some plasmids like R6K, initiate replication from specific origins and the replication forks moving either bi-or unidirectionally, are arrested at sequence-specific replication termini (1-3). Sequence-specific replication fork barriers have also been observed in the nontranscribed spacer regions of ribosomal DNAs of Saccharomyces cerevisiae (4, 5), plants (6), Xenopus (7), and human (8).The replication termini are sequence-specific and bind to cognate terminator proteins, and the protein-DNA complex arrests replication forks in an orientation-dependent manner (9, 10). DnaB (11,12,19). Detailed biochemical and biophysical analyses have been made possible in both the systems by the determination of the crystal structures of RTP at 2.6 Å (21) and of Tus-Ter () complex at 2.7 Å (22). The DNA binding (23), dimer-dimer interaction (24), and DnaB interaction domains (25) of RTP have been determined by genetic and biochemical analyses that used the crystal structure as a guide. Similarly, the DNA binding domain of Tus has been determined with the help of crystal structure and genetic analysis (22).The impact of transcription on the initiation (26, 27) and elongation stages of DNA replication have been reported (28,29). We have reported previously that Tus and RTP can block RNA chain elongation catalyzed by several prokaryotic RN...

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Section: Discussionmentioning

confidence: 82%

Section: Fate Of Tus Protein When Rnap Invades Tus-ter () Complex Fromentioning

confidence: 99%

Mechanistic Studies on the Impact of Transcription on Sequence-specific Termination of DNA Replication and Vice Versa

Mohanty

Sahoo

Bastia

1998

Journal of Biological Chemistry

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“…Such proteins could inhibit transcriptional elongation by a "roadblock" type mechanism as has been characterized in some prokaryotic systems (reviewed in Spencer and Groudine, 1990). No DNA binding proteins have so far been implicated in general transcriptional termination at sites downstream from pol TI-transcribed genes, although a well-characterized DNA binding activity mediates termination by eukaryotic RNA polymerase I (Kuhn et al, 1990;McStay and Reeder, 1990a;Pfleiderer et al, 1990;Smid et al, 1992). Similarly, no proteins have been shown to interact with RNA sequences at sites of premature termination.…”

Section: Regulation Of Transcriptional Elongation Within Eukaryotic Cmentioning

confidence: 99%

Regulation of eukaryotic gene expression by transcriptional attenuation.

Wright

1993

MBoC

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“…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.…”

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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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Specific interaction of the murine transcription termination factor TTF I with class-I RNA polymerases

Cited by 102 publications

References 16 publications

Mechanistic Studies on the Impact of Transcription on Sequence-specific Termination of DNA Replication and Vice Versa

Mechanistic Studies on the Impact of Transcription on Sequence-specific Termination of DNA Replication and Vice Versa

Regulation of eukaryotic gene expression by transcriptional attenuation.

Intrinsic Transcript Cleavage in Yeast RNA Polymerase II Elongation Complexes

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