Dr Basil Greber obtained his BSc and MSc in Biology from ETH Zurich, Switzerland. During his MSc thesis work in the laboratory of Professor Nenad Ban, he determined the structure of the Oxa1 membrane protein insertase bound to a bacterial ribosome using cryo-electron microscopy (cryo-EM).
This experience left him with a fascination for large and intricate macromolecular assemblies and a lasting interest in unraveling the molecular mechanisms by which they perform their functions.
After a 6-month stay in the laboratory of Professor Manuel Mendoza at the Centre for Genomic Regulation
in Barcelona to study chromosome segregation and cytokinesis in budding yeast, Dr Greber returned to the Ban laboratory for his doctoral thesis work to study the structure, function, and evolution of the ribosome.
At that time, the development of high-resolution cryo-EM transformed structural biology, and its application to the ribosomal complexes studied by Dr Greber resulted in a number of unexpected discoveries, including a built-in architectural tRNA in the mammalian mitochondrial ribosome and a new structural probing mechanism for the ribosomal tunnel during eukaryotic ribosome assembly. Dr Greber was awarded the Scaringe Award of the RNA Society
for these studies.
Subsequently, Dr Greber moved to the laboratory of Professor Eva Nogales at the University of California, Berkeley
as a postdoctoral fellow, supported by the Swiss National Science Foundation
. There, he determined the complete structure of human transcription factor TFIIH, a multifunctional protein complex that is critical both for transcription initiation and DNA repair throughout eukaryotes.
In summer 2020, he joined the ICR as an independent fellow to perform structural and functional studies of nucleotide excision repair (NER). Due to its critical cellular role, dysfunction of the NER pathway results in human disease, including cancer. Dr Greber's group aims to uncover the molecular mechanisms by which the pathway operates.