We are a basic research laboratory that studies the structural, biochemical, and functional basis for macromolecules involved in post-translational protein modification by ubiquitin and ubiquitin-like proteins such as SUMO, and pathways that contribute to co- and post-transcriptional RNA maturation, processing and decay. We pursue biochemical approaches to reconstitute key intermediates or complexes in these pathways and combine them with single particle cryo-EM and x-ray crystallography in conjunction with genetics and biochemistry to elucidate structure/activity relationships.
Christopher D. Lima, PhD
Research FocusThe Lima laboratory studies essential eukaryotic pathways that contribute to RNA processing and decay as well as post-translational protein modification by ubiquitin and ubiquitin-like modifiers such as SUMO.
EducationPhD, Northwestern University
- Weick, E.M., Puno, M.R., Januszyk, K., Zinder, J.C., DiMattia, M.A., Lima, C.D. Helicase-Dependent RNA Decay Illuminated by a Cryo-EM Structure of a Human Nuclear RNA Exosome-MTR4 Complex. Cell 173, 1663-1677 (2018)
- Wasmuth, E.V., Zinder, J.C., Zattas, D., Das, M., and Lima, C.D. Structure and reconstitution of yeast Mpp6-nuclear exosome complexes reveals that Mpp6 stimulates RNA decay and recruits the Mtr4 helicase. Elife Jul 25;6. pii: e29062. doi: 10.7554/eLife.29062 (2017)
- Fellow of the American Academy of Arts and Sciences (2017)
- Investigator, Howard Hughes Medical Institute (2013)
- Louise and Allston Boyer Young Investigator in Basic Research, Memorial Sloan Kettering Cancer Center (2006)
- Scholar, Rita Allen Foundation (2003-2006)
- Mayor's Award for Excellence in Science and Technology, NYC Department of Cultural Affairs and New York Academy of Sciences (2003)