The present proposal deals with the involvement of a protein, BTAF1 in transcription. This process is mediated by TBP (TATA-binding protein) containing complexes. Among them B-TFIID is unique in containing only one TBP interacting protein, BTAF1 and in exhibiting ATPase activity which regulates BTAF1-TBP interaction. Little is known about this regulation.
The proposal aims i) to identify new interactors of BTAF1 and to study effects of them on BTAF1 function both in transcription and in ATPase assays and ii ) to visualize conformational changes within B-TFIID. The host laboratory is the Laboratory for physiological Chemistry managed by Marc Timmers located at the University Medical Centre of Utrecht. During my Ph.D. work I gained experience in study of protein-protein interactions.
The new stimulating environment, which represents the host laboratory, will allow me to tackle this major question from another angle. In fact, in addition to significantly improve my skills in protein expression systems, purification and protein-protein interactions assays, I will learn to master new skills as protein/DNA interactions assays and transcription assays. Thanks to collaboration with an international group I will be able to use cryo-electron microscopy to study the topology of large protein complexes. This very fruitful experience will provide me the opportunity to find an academic position in France.
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