Roger David Kornberg was born on April 24, 1947. He is an American biochemist and a professor in the field of structural biology at Stanford University School of Medicine. In 2006, Kornberg was awarded the Nobel Prize in Chemistry for his research on how genetic information from DNA is copied into RNA, known as "the molecular basis of eukaryotic transcription."

Early life and education

Kornberg was born in St. Louis, Missouri, into a Jewish family. He was the oldest son of Arthur Kornberg, a biochemist who won the Nobel Prize, and Sylvy Kornberg, who was also a biochemist. Kornberg received his bachelor's degree in chemistry from Harvard University in 1967. He earned his Ph.D. in chemical physics from Stanford University in 1972, with guidance from Harden M. McConnell.

Career

Kornberg worked as a postdoctoral researcher at the Laboratory of Molecular Biology in Cambridge, England. In 1976, he became an Assistant Professor of Biological Chemistry at Harvard Medical School. In 1978, he moved to his current role as Professor of Structural Biology at Stanford Medical School. From 2004 to 2025, Kornberg was the editor of the Annual Review of Biochemistry. He is a member of the Board of Directors of Annual Reviews.

Research

Kornberg identified the role of RNA polymerase II and other proteins in DNA transcription, creating 3D images of the protein cluster using X-ray crystallography.

Kornberg and his research group made several important discoveries about the mechanisms and regulation of eukaryotic transcription. As a graduate student working with Harden McConnell at Stanford in the late 1960s, he discovered the "flip-flop" and lateral diffusion of phospholipids in bilayer membranes. Later, as a postdoctoral fellow working with Aaron Klug and Francis Crick at the MRC in the 1970s, Kornberg discovered the nucleosome, the basic protein complex that packages chromosomal DNA in the nucleus of eukaryotic cells (chromosomal DNA is often called "chromatin" when it is bound to proteins). Within the nucleosome, Kornberg found that about 200 base pairs of DNA are wrapped around an octamer of histone proteins. With Yahli Lorch, Kornberg showed that a nucleosome on a promoter prevents the initiation of transcription, leading to the recognition of a functional role for the nucleosome, which acts as a general gene repressor.

Kornberg's research group at Stanford later developed a faithful transcription system from baker's yeast, a simple unicellular eukaryote, and used it to isolate all the several dozen proteins needed for transcription in a purified form. Through Kornberg's work and that of others, it has become clear that these protein components are highly similar across all eukaryotes, from yeast to human cells.

Using this system, Kornberg discovered that gene regulatory signals are transmitted to the RNA polymerase machinery by an additional protein complex called Mediator. As noted by the Nobel Prize committee, "the great complexity of eukaryotic organisms is actually enabled by the fine interplay between tissue-specific substances, enhancers in the DNA, and Mediator. The discovery of Mediator is therefore a true milestone in the understanding of the transcription process."

At the same time as studying transcription, Kornberg spent two decades developing methods to visualize the atomic structure of RNA polymerase and its associated proteins. He used expertise with lipid membranes from his graduate studies to create a technique for forming 2D protein crystals on lipid bilayers. These crystals were analyzed with electron microscopy to produce low-resolution images of the protein's structure. Eventually, Kornberg used X-ray crystallography to determine the 3D structure of RNA polymerase at atomic resolution. He has since extended these studies to obtain images of RNA polymerase associated with accessory proteins. Through these studies, Kornberg created a detailed picture of how transcription works at the molecular level. According to the Nobel Prize committee, "the truly revolutionary aspect of Kornberg's picture is that it captures the process of transcription in full flow. What we see is an RNA strand being built, and hence the exact positions of the DNA, polymerase, and RNA during this process."

As a graduate student at Stanford University, Kornberg studied the rotation of phospholipids and defined the dynamics of lipids in the membrane for the first time. He called the movement of lipids from one membrane layer to another "flip-flop" because he had studied electronic circuit elements called flip-flops a few years earlier. This term led to the naming of proteins called flippases and floppases.

Kornberg has served on the Scientific Advisory Boards of the following companies: Cocrystal Discovery, Inc. (Chairman), ChromaDex Corporation (Chairman), StemRad, Ltd., Oplon Ltd. (Chairman), and Pacific Biosciences. He has also been a director for the following companies: OphthaliX Inc., Protalix BioTherapeutics, Can-Fite BioPharma, Ltd., Simploud, and Teva Pharmaceutical Industries, Ltd.