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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly. / Male, Gary; von Appen, Alexander; Glatt, Sebastian; Taylor, Nicholas M I; Cristovao, Michele; Groetsch, Helga; Beck, Martin; Müller, Christoph W.

In: Nature Communications, Vol. 6, 7387, 2015.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Male, G, von Appen, A, Glatt, S, Taylor, NMI, Cristovao, M, Groetsch, H, Beck, M & Müller, CW 2015, 'Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly', Nature Communications, vol. 6, 7387. https://doi.org/10.1038/ncomms8387

APA

Male, G., von Appen, A., Glatt, S., Taylor, N. M. I., Cristovao, M., Groetsch, H., Beck, M., & Müller, C. W. (2015). Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly. Nature Communications, 6, [7387]. https://doi.org/10.1038/ncomms8387

Vancouver

Male G, von Appen A, Glatt S, Taylor NMI, Cristovao M, Groetsch H et al. Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly. Nature Communications. 2015;6. 7387. https://doi.org/10.1038/ncomms8387

Author

Male, Gary ; von Appen, Alexander ; Glatt, Sebastian ; Taylor, Nicholas M I ; Cristovao, Michele ; Groetsch, Helga ; Beck, Martin ; Müller, Christoph W. / Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly. In: Nature Communications. 2015 ; Vol. 6.

Bibtex

@article{43c305a6c46c441d98a08025c9d0d9e6,
title = "Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly",
abstract = "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.",
keywords = "Crystallography, X-Ray, RNA Polymerase III/chemistry, Saccharomyces cerevisiae Proteins/chemistry, Tandem Mass Spectrometry, Transcription Factors, TFIII/chemistry",
author = "Gary Male and {von Appen}, Alexander and Sebastian Glatt and Taylor, {Nicholas M I} and Michele Cristovao and Helga Groetsch and Martin Beck and M{\"u}ller, {Christoph W}",
year = "2015",
doi = "10.1038/ncomms8387",
language = "English",
volume = "6",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly

AU - Male, Gary

AU - von Appen, Alexander

AU - Glatt, Sebastian

AU - Taylor, Nicholas M I

AU - Cristovao, Michele

AU - Groetsch, Helga

AU - Beck, Martin

AU - Müller, Christoph W

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

KW - Crystallography, X-Ray

KW - RNA Polymerase III/chemistry

KW - Saccharomyces cerevisiae Proteins/chemistry

KW - Tandem Mass Spectrometry

KW - Transcription Factors, TFIII/chemistry

U2 - 10.1038/ncomms8387

DO - 10.1038/ncomms8387

M3 - Journal article

C2 - 26060179

VL - 6

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 7387

ER -

ID: 194520528