Robert J. Tomko

Mapping interaction of assembly factor Rpn14 with the proteasome base reveals a bipartite interface and implies ordered remodeling of intersubunit contacts during proteasome biogenesis.

The 26S proteasome is the largest known protease and an essential mediator of targeted protein degradation, a transformative therapeutic modality for human diseases. Assembly of the 26S proteasome from its 66 cognate subunits depends on nine dedicated assembly chaperones. These chaperones generally function by stabiliz...