A suppressor of mutations in the class III transcription system encodes a component of yeast TFIIIB.

Rüth, Jochen; Conesa, Christine; Dieci, Giorgio; Lefebvre, Olivier; Düsterhöft, Andreas; Ottonello, Simone; Sentenac, André

doi:10.1002/j.1460-2075.1996.tb00545.x

Cited by 85 publications

(104 citation statements)

References 71 publications

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“…The association of Sub1 to all Pol III-transcribed genes in vivo and the previous observation of a stimulatory effect of PC4 on a human Pol III transcription system in vitro (13) prompted us to test the effect of Sub1 on in vitro transcription. A transcription system reconstituted with all recombinant factors and highly purified Pol III directs a low level of RNA synthesis and needs to be supplemented with partially purified fractions like BЈЈ (23) or TFIIIE (24,25) to restore strong transcription rates (26), suggesting the existence of positive auxiliary factors enhancing Pol III transcription. As shown in Fig.…”

Section: Sub1mentioning

confidence: 99%

Genome-wide location analysis reveals a role for Sub1 in RNA polymerase III transcription

Tavenet

Suleau

Dubreuil

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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Human PC4 and the yeast ortholog Sub1 have multiple functions in RNA polymerase II transcription. Genome-wide mapping revealed that Sub1 is present on Pol III-transcribed genes. Sub1 was found to interact with components of the Pol III transcription system and to stimulate the initiation and reinitiation steps in a system reconstituted with all recombinant factors. Sub1 was required for optimal Pol III gene transcription in exponentially growing cells.

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Section: Sub1mentioning

confidence: 99%

Genome-wide location analysis reveals a role for Sub1 in RNA polymerase III transcription

Tavenet

Suleau

Dubreuil

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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“…Nonetheless, although TDF is apparently distinct, we cannot exclude the formal possibility that it is a loosely associated subunit of one of the other factors. It might also be related to yeast transcription factor TFIIIE, which is reported to be required for transcription by highly purified yeast RNA Pol III, TFIIIC, and TFIIIB but not yet purified (Dieci et al 1993;Ruth et al 1996).…”

Section: A Novel Accessory Factor For Initiation By Rna Pol IIImentioning

confidence: 99%

Identification of an autonomously initiating RNA polymerase III holoenzyme containing a novel factor that is selectively inactivated during protein synthesis inhibition

Wang

Luo²,

Roeder³

1997

Genes Dev.

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Eukaryotic RNA polymerases I, II, and III (Pol I, Pol II, Pol III) are structurally distinct, transcribe distinct sets of genes in conjunction with distinct sets of general initiation factors, and respond to largely distinct gene-specific activators (for review, see Zawel and Reinberg 1995;Roeder 1996a). Despite these differences, some mechanistic similarities are apparent. The three RNA polymerases share five common subunits and other subunits that are highly related (Woychik et al. 1990;McKune et al. 1995;Shpakovski et al. 1995), whereas the TATA-binding protein (TBP) is shared by three RNA polymerase type-specific accessory factors (Struhl 1994). Studies with isolated components have shown ordered pathways for the assembly of RNA polymerases and cognate initiation factors into active preinitiation complexes (for review, see Zawel and Reinberg 1995;Roeder 1996a). In addition, there is a parallel between RNA Pol II recruitment by interaction with the TFIIB component of a TFIIB-TFIID-promoter complex (for review, see Roeder 1996b) and RNA Pol III recruitment by interaction with a TFIIB-related component of a TFIIIB-TFIIIC-promoter complex (Werner et al. 1993; Wang and Roeder 1997).Although the stepwise assembly of functional preinitiation complexes is readily demonstrated in vitro, recent studies have identified large complexes (RNA Pol II ''holoenzymes'') that contain RNA Pol II, some or all of the general initiation factors, and various cofactors (Kim et al.

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“…The L469K Mutation in TPRs6 -9 Affects Bdp1 BindingBdp1 and Tfc4 interact in binary assays (21,26) although the domain(s) of Tfc4 that direct the interaction have yet to be defined. Nonetheless, analysis of deletion mutants of Tfc4 (21,26), the synthetic lethal phenotype of the PCF1-1 mutant allele in a Bdp1⌬(355-372) strain (27) and the inability of a point mutation in TPR7 of Tfc4 to bind Bdp1 (28) all suggest that the TPR arrays contribute to the association between Tfc4 and Bdp1.…”

Section: Amino Acid Substitutions At Phylogenetically Conserved Positmentioning

confidence: 99%

“…The TPRs also contribute to the interaction between Tfc4 and the TFIIIB subunit Bdp1. Although the Bdp1-binding site(s) in Tfc4 has not yet been defined, analysis of deletion mutants of Tfc4 (21,26) and the effect of amino acid substitutions in both TPR2 (27) and TPR7 (28) suggest that the TPR arrays are involved in the association between Tfc4 and Bdp1. The TPRs in Tfc4 may therefore provide binding sites for multiple ligands.…”

mentioning

confidence: 99%

The Brf1 and Bdp1 Subunits of Transcription Factor TFIIIB Bind to Overlapping Sites in the Tetratricopeptide Repeats of Tfc4

Liao

Willis

Moir

2003

Journal of Biological Chemistry

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The RNA polymerase III initiation factor TFIIIB is assembled onto DNA through interactions involving the Tfc4 subunit of the assembly factor TFIIIC and two subunits of TFIIIB, Brf1 and Bdp1. Tfc4 contains two arrays of tetratricopeptide repeats (TPRs), each of which provides a binding site for Brf1. Dominant mutations in the ligand binding channel of the first TPR array, TPRs1-5, and on the back side of this array, increase Brf1 binding by Tfc4. Here we examine the biological importance of the second TPR array, TPRs6 -9. Radical mutations at phylogenetically conserved residues in the ligand binding channel of TPRs6 -9 impair pol III reporter gene transcription. Biochemical studies on one such mutation, L469K in TPR7, revealed a defect in the recruitment of Brf1 into TFIIIB-TFIIIC-DNA complexes and diminished the direct interaction between Tfc4 and Brf1. Multicopy suppression analysis implicates TPR9 in Brf1 binding and TPRs7 and 8 in binding to more than one ligand. Indeed, the L469K mutation also decreased the binding affinity for Bdp1 incorporation into TFIIIB-TFIIIC-DNA complexes and inhibited binary interactions between Bdp1 and Tfc4. The Bdp1 binding domain in Tfc4 was mapped to TPRs1-9, a domain that contains both TPR arrays and thus overlaps two of the known binding sites for Brf1. The properties of the L469K mutation identify both Brf1 and Bdp1 as ligands for the second TPR array.The assembly of the initiation factor TFIIIB by TFIIIC is a limiting step in RNA polymerase III (pol III) 1 transcription. Although multiple subunits of both TFIIIB and TFIIIC interact (1-4) TFIIIB assembly is mediated initially by protein-protein interactions between the TFIIIC subunit, Tfc4, and the TFIIIB subunit, Brf1. Biochemical and genetic studies in yeast indicate that the recruitment of Brf1 by TFIIIC is a major limiting step in preinitiation complex assembly (5-7). Subsequent binding of the TBP and Bdp1 subunits of TFIIIB generates a series of structural changes in Tfc4, Brf1 and DNA that leads to progressively increased accessibility of Brf1 to DNA (8). The protein-protein interactions between TFIIIB subunits, together with DNA bending, generate a highly stable TFIIIB complex, a structure that surrounds and kinetically traps the DNA (9 -12).Tfc4 contains eleven copies of a ubiquitous protein-protein interaction motif known as a tetratricopeptide repeat (13,14).TPR motifs, as the name implies, are typically 34 amino acids in length and fold into two antiparallel ␣-helices (designated A and B, Ref. 15). Although no position within the motif is invariant, a pattern of small and large hydrophobic residues defines the loose TPR consensus and provides stacking interactions between adjacent repeats (15-17). Multiple adjacent repeats form a right-handed superhelix in which the inner channel (formed by the A-helices) provides a ligand binding interface (18 -20). The TPRs in Tfc4 are organized into two arrays in the N terminus, TPR1-5 and TPR6 -9 (with five and four repeats, respectively) that are separated by a region of mini...

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A suppressor of mutations in the class III transcription system encodes a component of yeast TFIIIB.

Cited by 85 publications

References 71 publications

Genome-wide location analysis reveals a role for Sub1 in RNA polymerase III transcription

Genome-wide location analysis reveals a role for Sub1 in RNA polymerase III transcription

Identification of an autonomously initiating RNA polymerase III holoenzyme containing a novel factor that is selectively inactivated during protein synthesis inhibition

The Brf1 and Bdp1 Subunits of Transcription Factor TFIIIB Bind to Overlapping Sites in the Tetratricopeptide Repeats of Tfc4

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