Human Genome Project Information. Click to return to home page.

Sponsored by the U.S. Department of Energy Human Genome Program

Human Genome News Archive Edition
Vol. 11, No. 1-2, November 2000
Available in PDF
 
In this issue...

HGP and the Private Sector

HGP Milestones

In the News

Ethical, Legal, and Social Issues

Web, Publications, Resources

Funding

Meeting Calendars & Acronyms

  • Genome and Biotechnology Meetings
  • Training Courses and Workshops
  • Acronyms

HGN archives and subscriptions
Human Genome Project Information home

High-Resolution Image Reveals Structure of Protein Machine

Using a high-energy X-ray beam from the National Synchrotron Light Source (NSLS) at Brookhaven National Laboratory, researchers at Yale University and the Howard Hughes Medical Institute obtained the most detailed images ever seen of the ribosome (the protein-making structure inside all living cells). NSLS is a DOE Office of Biological and Environmental Research structural biology user facility.

In prokaryotes (bacteria and other simple organisms) as well as the more complex eukaryotes, ribosomes help translate gene-encoded information into a specific protein. Ribosomes consist of two unequally sized subunits containing RNA and proteins. The smaller component binds the messenger RNA (mRNA), which contains genetic instructions that specify the amino acids required to build a particular protein. The larger ribosomal subunit attaches one amino acid to the next in the growing protein chain.

In the August 11 issue of Science, investigators reported visualizing the atomic structure of the bacterium Haloarcula marismortuis larger ribosomal subunit at an unprecedented resolution of 2.4 Å. Until this report was published, researchers did not know whether ribosomal RNA or protein was responsible for catalyzing link formation. The new images revealed the proteins deeply embedded in the RNA and their essential role in its folding. The images also showed where binding takes place, proving RNAs ability to break or form bonds. Further studies should show the orientation of mRNA and the growing proteins components in the ribosomes active catalytic site.

In this study, researchers used the 2.5-billion-electron volt beam to perform crystallography on painstakingly grown crystals of the 50S subunits. Additional data were gathered using the Advanced Photon Source at Argonne National Laboratory.

During X-ray crystallography, intense beams pass through and bounce off atoms in the crystal, where they leave a diffraction pattern that can be analyzed to determine the proteins 3-D shape. Researchers resolved the atomic structures of all 100,000 or so crystal atoms in the RNA 50S subunit. This involved carefully growing larger, more complete ribosome crystals and solving their structures at progressively higher resolutions. Each level provided information that helped scientists understand the final high-resolution map.


The electronic form of the newsletter may be cited in the following style:
Human Genome Program, U.S. Department of Energy, Human Genome News (v11n1-2).

Return to Top of Page

Acronym List

Human Genome Project 1990–2003

The Human Genome Project (HGP) was an international 13-year effort, 1990 to 2003. Primary goals were to discover the complete set of human genes and make them accessible for further biological study, and determine the complete sequence of DNA bases in the human genome. See Timeline for more HGP history.

Human Genome News

Published from 1989 until 2002, this newsletter facilitated HGP communication, helped prevent duplication of research effort, and informed persons interested in genome research.