TY  - GEN
N2  - Transcription Factor IIIC (TFIIIC) is a six-subunit protein complex that recognises highly conserved promoter elements within genes transcribed by RNA polymerase III. These promoter elements, called ?A box? and ?B box?, are recognised by two subcomplexes of TFIIIC, termed ??A? and ??B?. The ?A subcomplex is formed from three subunits: ?131, ?95 and ?55. The ?B subcomplex is also composed of three subunits: ?138, ?91 and ?60. The binding of TFIIIC to these promoter elements leads to the recruitment of another transcription factor, TFIIIB, which subsequently coordinates the recruitment of RNA polymerase III to the transcription start site. 
In this thesis, I present my work on the characterisation of a novel interface between the ?A and ?B subcomplexes, which is located between the subunits ?131 and ?138. Chemical cross-linking coupled with mass spectrometry provides evidence for an important interaction between these two essential proteins, which I have mapped in detail using biochemical, biophysical and structural methods. The structure of a highly conserved tetra-trico peptide repeat (TPR) domain within ?131 is presented and is shown to bind with high affinity to a disordered region of ?138. In addition, I present the first high resolution structure of an extended winged helix domain of ?138 that I have solved by X-ray crystallography. Finally, I present work detailing efforts to produce the TFIIIC complex recombinantly in insect cells. The work presented here will further our understanding of the architecture of TFIIIC and provide insight into TFIIIC structure and function. 

UR  - https://archiv.ub.uni-heidelberg.de/volltextserver/17692/
A1  - Male, Gary
ID  - heidok17692
TI  - Insights into the Architecture of Transcription Factor IIIC
Y1  - 2014///
AV  - public
ER  -