James Williamson

Dr. James Williamson is the Executive Vice President of Research and Academic Affairs at The Scripps Research Institute, as well as a Professor in the Departments of Chemistry and Integrative Structural & Computational Biology. His research involves the study of RNA structure, RNA-protein interactions and RNA-ligand interactions using biochemistry, biophysics and structural biology approaches.


Among his many early scientific career accomplishments, Dr. Williamson was named a Searle Scholar, a Rita Allen Scholar, a Camille Dreyfus Teacher-Scholar, a Sloan Research Fellow and was awarded a Jane Coffin Childs Postdoctoral Fellowship. His studies have appeared in more than 200 peer-reviewed publications and in 2010, he was elected to the American Academy of Arts and Sciences. He currently serves on editorial boards for a number of top scientific journals and professional societies.


At Scripps Research, Dr. Williamson continues to successfully execute multiple leadership roles, especially those encompassing academic planning and training. In 2001, he was named Associate Dean for the Chemistry program and from 2008-2017, he was the Dean of Graduate and Postdoctoral Studies for the Institute’s nationally ranked graduate program. He was named Vice President of Academic Affairs in 2015 and appointed Executive Vice President in 2017.


Dr. Williamson earned his doctorate in chemistry at Stanford University in 1988. Following postdoctoral work at the University of Colorado, he joined the faculty of the Chemistry department at the Massachusetts Institute of Technology, where he attained the rank of associate professor with tenure. He accepted an appointment to The Scripps Research Institute as a professor in 1998.

Ribosome Assembly in Bacteria

Ribosomes are responsible for all protein synthesis in cells, and the process of assembling ribosomes accounts for one third of the energy budget for rapidly growing bacteria.  The assembly process involves coordination of synthesis of three large ribosomal RNAs and fifty ribosomal proteins in an incredibly efficient process that requires about two minutes in cells.  Assembly is guided by over fifty assembly factors that are chaperones and modification enzymes, but we have a basic and emerging understanding of the steps involved in making a ribosome.  Our laboratory uses a wide variety of biophysical methods to characterize the structure and dynamics of assembling ribosomes in vitro, and in cells.  Quantitative mass spectrometry reveals the composition of intermediates, electron microscopy reveals the heterogeneous distribution of assembly intermediates, and single molecule fluorescence reveals the dynamics of structural transitions that occur during assembly.  The overall picture that is emerging is that there are parallel pathways for installation of various structural units, but that certain events must happen in a particular order.  The parallel and sequential nature of assembly appears to be an optimal balance for efficient and accurate assembly.  This talk will describe recent advances in our understanding of ribosome assembly in bacteria, focusing on general principles that are emerging about the extensive RNA folding that is at the heart of the process.