Structural and Functional Characterization of a Phosphatase Domain within Yeast General Transcription Factor IIIC

Taylor, Nicholas M. I.; Glatt, Sebastian; Hennrich, Marco L.; Scheven, Gudrun von; Fernández‐Tornero, Carlos; Rybin, Vladimir; Gavin, Anne‐Claude; Kolb, Peter; Müller, Christoph W.

doi:10.1074/jbc.m112.427856

Cited by 13 publications

(14 citation statements)

References 43 publications

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“… 12 ), and the τ95 DNA-binding domain (DBD) 14 and τ95–τ55 dimerization homologues from S. pombe 14 . Note that the non-conserved τ55 histidine phosphatase domain (HPD) is omitted 13 . The extended N terminus and C-terminal TPRs of τ131 are indicated schematically.…”

Section: Figurementioning

confidence: 99%

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Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly

et al. 2015

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In eukaryotes, RNA Polymerase III (Pol III) is specifically responsible for transcribing genes encoding tRNAs and other short non-coding RNAs. The recruitment of Pol III to tRNA-encoding genes requires the transcription factors (TF) IIIB and IIIC. TFIIIC has been described as a conserved, multi-subunit protein complex composed of two subcomplexes, called τA and τB. How these two subcomplexes are linked and how their interaction affects the formation of the Pol III pre-initiation complex (PIC) is poorly understood. Here we use chemical crosslinking mass spectrometry and determine the molecular architecture of TFIIIC. We further report the crystal structure of the essential TPR array from τA subunit τ131 and characterize its interaction with a central region of τB subunit τ138. The identified τ131–τ138 interacting region is essential in vivo and overlaps with TFIIIB-binding sites, revealing a crucial interaction platform for the regulation of tRNA transcription initiation.

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Section: Figurementioning

confidence: 99%

“…While a significant amount of high-resolution structural and functional information exists for some individual TFIIIC subunits 12 13 14 , a detailed understanding of how the τA and τB subcomplexes are connected and which subunits could act as a flexible linker remains elusive ( Fig. 1a ).…”

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confidence: 99%

Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly

et al. 2015

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“…In addition, they have both been found to form a subcomplex of unknown function that occurs independently of holoTFIIIC (9). The conserved C-terminal part of τ55 was shown to be sufficient for the τ95-τ55 interaction, whereas the non-conserved N-terminal histidine phosphatase domain is not required (10,11). In the τB subcomplex, subunits τ60 and τ91 both form WD40 propellers that are perpendicularly packed against each other (12).…”

Section: Introductionmentioning

confidence: 99%

RNA polymerase III-specific general transcription factor IIIC contains a heterodimer resembling TFIIF Rap30/Rap74

Taylor

Baudin

Scheven

et al. 2013

Nucleic Acids Research

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Transcription of tRNA-encoding genes by RNA polymerase (Pol) III requires the six-subunit general transcription factor IIIC that uses subcomplexes τA and τB to recognize two gene-internal promoter elements named A- and B-box. The Schizosaccharomyces pombe τA subcomplex comprises subunits Sfc1, Sfc4 and Sfc7. The crystal structure of the Sfc1/Sfc7 heterodimer reveals similar domains and overall domain architecture to the Pol II-specific general transcription factor TFIIF Rap30/Rap74. The N-terminal Sfc1/Sfc7 dimerization module consists of a triple β-barrel similar to the N-terminal TFIIF Rap30/Rap74 dimerization module, whereas the C-terminal Sfc1 DNA-binding domain contains a winged-helix domain most similar to the TFIIF Rap30 C-terminal winged-helix domain. Sfc1 DNA-binding domain recognizes single and double-stranded DNA by an unknown mechanism. Several features observed for A-box recognition by τA resemble the recognition of promoters by bacterial RNA polymerase, where σ factor unfolds double-stranded DNA and stabilizes the non-coding DNA strand in an open conformation. Such a function has also been proposed for TFIIF, suggesting that the observed structural similarity between Sfc1/Sfc7 and TFIIF Rap30/Rap74 might also reflect similar functions.

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“…This result confirmed the hypothesis that the three nuclear RNA polymerases share a TFIIF-like dimerization module, further showing how relevant biological information can be extracted from low-resolution crystallographic experiments. Interestingly, a similar module has been found in TFIIIC, a Pol IIIspecific transcription factor (Taylor et al, 2013).…”

Section: Experimental Phasing and Density Modificationmentioning

confidence: 57%

Solving the RNA polymerase I structural puzzle

Moreno-Morcillo

Taylor

Gruene

et al. 2014

Acta Crystallogr D Biol Crystallogr

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Structural and Functional Characterization of a Phosphatase Domain within Yeast General Transcription Factor IIIC

Cited by 13 publications

References 43 publications

Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly

Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly

RNA polymerase III-specific general transcription factor IIIC contains a heterodimer resembling TFIIF Rap30/Rap74

Solving the RNA polymerase I structural puzzle

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