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