Variants of the TATA-binding protein can distinguish subsets of RNA polymerase I, II, and III promoters

Schultz, Michael C.; Reeder, Ronald H.; Hahn, Steven

doi:10.1016/0092-8674(92)90233-3

Cited by 224 publications

(158 citation statements)

References 24 publications

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“…This had not been formally tested previously. Finally, a series of oligonucleotide and antibody inhibition studies suggest that TBP is assembled in distinct ways in the three transcription systems, as has been suggested previously (42,44).…”

Section: Discussionmentioning

confidence: 79%

“…This extends the phylogenetic range in which this is true beyond human (reviewed in reference 42) and yeast (7,44) cells. Second, we verified that TBP is a component of A. castellanii rRNA transcription factor TIF-IB.…”

Section: Discussionmentioning

confidence: 95%

“…This approach began to change when it was discovered that some of the genes for small nuclear RNAs (snRNAs) are transcribed by polymerase III whereas most are transcribed by polymerase II (27,32,35,47 The full impact of this factor overlap was perhaps not realized because polymerase I still appeared to use dedicated factors. However, a flurry of studies (6,7,44,56) revealed that TBP was required for transcription of all genes. TBP is now known to be a subunit of TFIID (41), TFIIIB (17,24,48,55), and human TIF-IB (SL1) (6).…”

mentioning

confidence: 99%

“…However, a flurry of studies (6,7,44,56) revealed that TBP was required for transcription of all genes. TBP is now known to be a subunit of TFIID (41), TFIIIB (17,24,48,55), and human TIF-IB (SL1) (6).…”

mentioning

confidence: 99%

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TATA box-binding protein (TBP) is a constituent of the polymerase I-specific transcription initiation factor TIF-IB (SL1) bound to the rRNA promoter and shows differential sensitivity to TBP-directed reagents in polymerase I, II, and III transcription factors.

Radebaugh¹,

Matthews²,

Geiss³

et al. 1994

Mol. Cell. Biol.

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The role of the Acanthamoeba casteUlanii TATA-binding protein (TBP) in transcription was examined. Specific antibodies against the nonconserved N-terminal domain of TBP were used to verify the presence of TBP in the fundamental transcription initiation factor for RNA polymerase I, TIF-IB, and to demonstrate that TBP is part of the committed initiation complex on the rRNA promoter. The same antibodies inhibit transcription in all three polymerase systems, but they do so differentially. Oligonucleotide competitors were used to evaluate the accessibility of the TATA-binding site in TIF-IB, TFIID, and TFIIIB. The results suggest that insertion of TBP into the polymerase II and III factors is more similar than insertion into the polymerase I factor.While the transcription systems of eukaryotic RNA polymerases I, II, and III obviously share some characteristics, initiation mechanisms for these transcription systems have been largely studied separately. The polymerases themselves have five subunits in common, seven in the case of the "odd pols," RNA polymerases I and III (45). Nevertheless, the general transcription factors involved with each polymerase have been examined in isolation, perhaps masking important generalizations about their functions. This approach began to change when it was discovered that some of the genes for small nuclear RNAs (snRNAs) are transcribed by polymerase III whereas most are transcribed by polymerase II (27,32,35,47 The full impact of this factor overlap was perhaps not realized because polymerase I still appeared to use dedicated factors. However, a flurry of studies (6,7,44,56) revealed that TBP was required for transcription of all genes. TBP is now known to be a subunit of TFIID (41), TFIIIB (17,24,48,55), and human TIF-IB (SL1) (6). TBP is associated with additional subunits (TAFs) to make up the functional factors (reviewed in reference 41). The TAFs appear to be different for each polymerase system (reviewed in reference 42), although overlap of TAFs has not been rigorously ruled out. All the TBP-containing factors are pivotal for their respective polymerases. Indeed, TFIIIB and TIF-IB are fundamental transcription factors; i.e., they appear to be responsible for the repetitive recruitment of RNA polymerase during successive rounds of initiation (16; reviewed in references 36 and 37).The manner by which the TBP-containing factor is recruited to the promoter differs from gene to gene. For RNA polymerase III genes with type I (SS RNA) or type II (tRNA, VAI, Alu, EBER, 7SL, 4.5S) internal control regions, additional general transcription factors are required to assemble TFIIIB onto the promoter (reviewed in references 10-12). Initiation complex formation on 5S and tRNA genes is an organized process in which the factors bind in an obligatory order, each relying on protein-DNA and protein-protein interactions with a previously bound factor(s) to join the complex. On some genes the DNA interaction site for TFIIIB is sequence specific, whereas on others specific sequence recognition is no...

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Section: Discussionmentioning

confidence: 79%

Section: Discussionmentioning

confidence: 95%

mentioning

confidence: 99%

mentioning

confidence: 99%

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TATA box-binding protein (TBP) is a constituent of the polymerase I-specific transcription initiation factor TIF-IB (SL1) bound to the rRNA promoter and shows differential sensitivity to TBP-directed reagents in polymerase I, II, and III transcription factors.

Radebaugh¹,

Matthews²,

Geiss³

et al. 1994

Mol. Cell. Biol.

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“…TATA-binding protein (TBP) is a universal transcription factor for all eukaryotic genes (1)(2)(3). It recognizes and binds to promoter sequences, commits the fomation of preinitiation complexes, and allows transcription initiation via interaction with various basal transcription factors and RNA polymerases.…”

Section: Introductionmentioning

confidence: 99%

Multimerization of the mouse TATA-binding protein (TBP) driven by its C-terminal conserved domain

Kato

Makino²,

Kishimoto³

et al. 1994

Nucl Acids Res

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The conformational states of the mouse TATA-binding protein (TBP) in solution were studied. A histidine tag and a factor Xa recognition site-carrying mouse TBP was expressed in E.coli, highly purified, and its fundamental functions as a TBP were demonstrated. We analyzed the molecular states of mouse TBP by gel filtration and glycerol gradient sedimentation, and found that TBP forms heterogeneous multimers in solution. Direct binding of TBP molecules to each other was proven by the far-Western procedure. Analyses using TBPs truncated at the N-and C-termini demonstrated that the functionally important C-terminal domain was responsible for homomultimer formation, and the N-terminal domain enhances multimerization. Furthermore, it was found that the TATA sequence dissociates homomultimers, and only monomeric TBP binds to the TATA-box. We suggest that TBP shares structural motifs in the C-terminal conserved domain for intermolecular interaction and TATA-binding.

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Distinct TFIID complexes mediate the effect of different transcriptional activators.

et al. 1993

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Multiple chromatographically separable complexes containing the TATA binding protein (TBP), which exhibit different functional properties, exist in HeLa cells. At least three distinct subpopulations of such complexes can be functionally defined as TFIID since they function with RNA polymerase II. Using a partially reconstituted HeLa cell in vitro transcription system and immunoprecipitation with a monoclonal antibody directed against TBP, we show that stimulation of transcription by the chimeric activators GAL‐VP16, GAL‐TEF‐1 and GAL‐ER(EF) requires the presence of factors which are tightly associated with these TFIID complexes. Moreover, the activity of GAL‐TEF‐1 appears to be mediated by at least two chromatographically distinct populations of TFIID. The factor(s) associated with one of these populations is also required for the activity of GAL‐ER (EF) and GAL‐VP16, while the factor(s) associated with the other population functions selectively with GAL‐TEF‐1. These two TFIID populations are composed of both common and unique TBP associated factors (TAFs).

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Variants of the TATA-binding protein can distinguish subsets of RNA polymerase I, II, and III promoters

Cited by 224 publications

References 24 publications

TATA box-binding protein (TBP) is a constituent of the polymerase I-specific transcription initiation factor TIF-IB (SL1) bound to the rRNA promoter and shows differential sensitivity to TBP-directed reagents in polymerase I, II, and III transcription factors.

TATA box-binding protein (TBP) is a constituent of the polymerase I-specific transcription initiation factor TIF-IB (SL1) bound to the rRNA promoter and shows differential sensitivity to TBP-directed reagents in polymerase I, II, and III transcription factors.

Multimerization of the mouse TATA-binding protein (TBP) driven by its C-terminal conserved domain

Distinct TFIID complexes mediate the effect of different transcriptional activators.

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