Juli Feigon

Juli Feigon

1 (310) 825-9232

Laboratory Address:
Mol Sci Bldg 1429
Paul Boyer Hall 270

Lab Number:
1 (310) 206-3493

Mailing Address:
607 Charles Young Dr. East
P.O. Box 951569
Los Angeles, CA 90095

Fax Number:
(310) 825-0982

Work Address:
Paul Boyer Hall 241

Work Phone Number:
1 (310) 206-6922


Lab Director, Feigon Lab
Professor, Chemistry and Biochemistry, Biochemistry, Molecular Biology
Member, Biochemistry, Biophysics & Structural Biology GPB Home Area, California NanoSystems Institute, Molecular Biology Institute
Staff, NMR Core (DOE), Nuclear Magnetic Resonance (NMR) Core Facility (DOE)
Researcher, Biochemistry, Biophysics and Structural Biology, Development and Gene Regulation

Research Interests

We study nucleic acid structure and specific recognition of nucleic acids by proteins. Our primary research tool is multidimensional nuclear magnetic resonance (NMR) spectroscopy. We also utilize a range of molecular biology, biochemical, and biophysical techniques including X-ray crystallography. These techniques are used to determine the three-dimensional structures of DNA and RNA, to investigate their interactions with various proteins and ligands, and to study nucleic acid folding. One major area of investigation involves structural and functional studies of nucleic acids and proteins involved in eukaryotic ribosome biogenesis and in trafficking through the nucleolus. Major proteins and RNAs which we are investigating are nucleolin and its interaction with pre-ribosomal RNA, yeast RNAse III, and box H/ACA snoRNPs, which are involved in pseudouridylation of sites on the rRNA. We are also interested in the structure of DNA telomeres and their synthesis by telomerase. We determined the first structure of a telomere repeat DNA and showed that it forms a four-stranded G-quadruplex structure. Our current work is focused on determining structures of sub-domains of the telomerase RNA, including the H/ACA box region which targets telomerase to the nucleolus or Cajal bodies, and their interaction with telomerase proteins. Another area of interest is in the interaction of non-sequence specific HMG box proteins with DNA. These proteins have been shown to play roles in DNA recombination, repair, activation and repression of transcription as well as nucleosome assembly and disassembly. We are investigating how the yeast HMG box protein NHP6A interacts with DNA and modulates the affects of the anticancer drug cis-platin. We are also investigating the interactions of the DNA nucleotide excision repair protein HHR23A with other cellular DNA repair proteins, the ubiquitin/proteosome pathway, and HIV-1 Vpr. Finally, we are interested in fundamental questions of nucleic acid folding and cation interactions. We are also involved in NMR methods development to augment our studies of nucleic acid structure and cation interactions.


Dr. Feigon received her B.A. from Occidental College and her M.S. and Ph.D. from the University of California, San Diego where she studied with Dr. David Kearns. Her postdoctoral work was completed at the Massachusetts Institute of Technology, where she was a Damon Runyon-Walter Winchell Cancer Fund Postdoctoral Fellow with Dr. Alex Rich. Dr. Feigon joined the UCLA faculty in 1985.


A selected list of publications: