ERROR 1
ERROR 1
ERROR 2
ERROR 2
ERROR 2
ERROR 2
ERROR 2
Password and Confirm password must match.
If you have an ACS member number, please enter it here so we can link this account to your membership. (optional)
ERROR 2
ACS values your privacy. By submitting your information, you are gaining access to C&EN and subscribing to our weekly newsletter. We use the information you provide to make your reading experience better, and we will never sell your data to third party members.
Two groups have unraveled a bit more of the mystery of an enzyme that helps transcribe genetic information from DNA to RNA. The researchers have obtained long-sought crystal structures of the eukaryotic enzyme RNA polymerase I (Pol I), a key step toward figuring out how the enzyme works. Eukaryotes have three RNA polymerases—Pol I, II, and III—which transcribe genomic DNA into ribosomal RNA, messenger RNA, and transfer RNA, respectively. Roger D. Kornberg of Stanford University won the 2006 Nobel Prize in Chemistry for determining crystal structures and the mechanism of Pol II. Low-resolution electron microscopy images of Pol I and Pol III had revealed those enzymes’ overall architectures, but their atomic-level structures have been unavailable. Now, atomic-resolution crystal structures of Pol I have been obtained by Carlos Fernández-Tornero of the Spanish National Research Council, Madrid, Christoph W. Müller of the European Molecular Biology Laboratory, Heidelberg, and coworkers and by a team led by Patrick Cramer of the University of Munich (Nature 2013, DOI: 10.1038/nature12636 and 10.1038/nature12712). In a commentary, Joost Zomerdijk of the University of Dundee, in Scotland, says the studies could lead to “a picture of the specific mechanisms and control of ribosomal RNA-gene transcription in eukaryotes.”
Join the conversation
Contact the reporter
Submit a Letter to the Editor for publication
Engage with us on Twitter