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Carl C. Correll, PhD

Associate Professor

Dr. Carl C. Correll received a PhD in biological chemistry from the University of Michigan in 1992. From 1992 to 1997, he worked as a postdoctoral researcher at Yale University. He was an associate professor of biochemistry and molecular biology at the University of Chicago from 1998 to 2004.

Dr. Correll is a fellow of the American Cancer Society.


Interaction between protein and RNA is central to cellular and viral processes ranging from expressing genes to directing cell mortality. These processes are highly dynamic in involving RNA-RNA and RNA-protein structural rearrangements. Yet it remains poorly understood how these processes are directed and regulated. Together with our collaborator Dr. Johnson (University of Texas, Austin), we identify and investigate the function of proteins that are essential for ribosome biogenesis—a vital cellular process that is emerging as an unexplored target for cancer treatment.

Current Research Projects In The Correll Lab

One project is to investigate the mechanism by which the DEAH helicase Dhr1 dislodges U3 from the pre-ribosome, a key step in ribosome biogenesis. We have a paper in press at PLOS Biology that identifies Dhr1 as the helicase that dislodges U3 from the pre-rRNA in vivo and we show in vitro that Dhr1 unwinds U3-pre-rRNA duplexes in a mechanism reminiscent of DEAD box proteins. We are a subcontractor for Dr. Johnson on an NIH grant entitled “Biogenesis of the Small Ribosomal Subunit in Eukaryote”, which is funded until February 28, 2018.

A second project is to investigate the regulation of Dhr1 by Utp14 and the regulation of Imp3 and Imp4 by Mpp10. This project is a collaboration with Drs. Johnson and Jin (DePaul University). This is funded by a DePaul-RFUMS Research Pilot Grant project entitled "Assembly of Essential Complexes for Eukaryotic Ribosome Biogenesis" and is funded until November 30, 2015.

Lab Personnel

  • Carl Correll, PhD, Principal Investigator
  • Xiaomeng Shao, Research Assistant

Lab Alumni

  • Jutta Beneken Heller, PhD. After her postdoc in the Correll Lab, Jutta became an Instructor and Research Fellow in the Department of Biology at Loyola University of Chicago.
  • Timea Gerczei, PhD. After her postdoc in the Correll Lab, Timea became a tenure track faculty member in the Chemistry Department at Ball State University, Muncie, IN.
  • Matt Plantinga, PhD. Matt is a postdoctoral research with Prof. Dominique Broccoli at the Curtis and Elizabeth Anderson Cancer Institute.
  • Binal Shah, PhD. Research Associate.
  • Muralidhar Tata, MS. Muralidhar works as a Molecular Biologist at Novus International in Lincoln, Nebraska.


For e-Print (PDF File) contact Carl Correll.

  • Zhu, J., Liu, X., Anjos, M., Correll, C.C., Johnson, A.W. (2016) Utp14 recruits and activates the RNA helicase Dhr1 to undock U3 snoRNA from the pre-ribosome. Molecular and Cellular Biology 36, 965-978. [PubMed]
  • Sardana R., Liu, X., Granneman S., Zhu J., Gill, M., Papoulas, O., Marcotte, E.M., Tollervey, D., Correll, C.C., Johnson, A.W. (2015) The DEAH-box helicase Dhr1 Dissociates U3 from the pre-rRNA to promote formation of the Central Pseudoknot. PLoS Biology 13, e1002083. [PubMed]
  • Shah, B.N., Liu X., Correll C.C. (2013) Imp3 unfolds stem structures in pre-rRNA and U3 snoRNA to form a duplex essential for small subunit processing. RNA 19, 1372-1383. [PubMed]
  • Plantinga, M.J., Korennykh, A.V., Piccirilli, J.A., Correll, C.C. (2011) The ribotoxin restrictocin recognizes its RNA substrate by selective engagement of active site residues. Biochemistry 50, 3004-3013. [PubMed]
  • Gérczei, T., Shah, B.N., Anthony J. Manzo, A.J., Walter, N.G. and Correll, C.C. (2009) RNA chaperones stimulate formation and yield of the U3 snoRNA-pre-rRNA duplexes needed for ribosome biogenesis. Journal of Molecular Biology 390, 991-1006. [PubMed]
  • Plantinga, M.J., Korennykh, A.V., Piccirilli, J.A. and Correll, C.C. (2008) Electrostatic interactions guide the active site face of a structure-specific ribonuclease to its RNA substrate. Biochemistry 47, 8912-8918. [PubMed]
  • Korennykh AV, Plantinga MJ, Correll CC, Piccirilli JA. (2007) Abstract Linkage between Substrate Recognition and Catalysis during Cleavage of Sarcin/Ricin Loop RNA by Restrictocin. Biochemistry 46, 12744-12756. [PubMed]
  • Korennykh, A.V., Correll, C.C. and Piccirilli, J.A. (2007) Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins. RNA 13, 1391-1396. [PubMed]
  • Korennykh, A.V., Piccirilli, J.A. and Correll, C.C. (2006) The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins. Nature Structural & Molecular Biology 13, 436-443. [PubMed]
  • Gérczei, T. and Correll, C.C. (2004) Imp3p and Imp4p mediate formation of essential U3-pre-rRNA duplexes, possibly to recruit the small subunit processome to the pre-rRNA. PNAS 101, 15301-15306. [PubMed]
  • Correll, C.C., Beneken, J., Plantinga, M.J., Lubbers, M and Chan, Y-L (2003) The common and the distinctive features of the bulged-G motif based on a 1.04 Å resolution RNA structure. Nucleic Acids Research 31, 6806-6818.[PubMed]
  • Correll, C.C. and Swinger, K. (2003) Common and distinctive features of GNRA tetraloops based on a GUAA tetraloop structure at 1.4 Å resolution. RNA 9 355-363.[PubMed].


Chicago Medical School

  • Gene expression, regulation and dysregulation (i.e. cancer) in Clinical Molecular and Cell Biology MBCH502
  • Blood coagulation, blood groups, hemoglobin, hemoglobinopathies and iron metabolism in Medical Biochemistry MBCH505A
  • Population genetics in Clinical Genetics MBCH508
  • Course director of LGBTQI Healthcare, a sophomore elective MFPM600

All of the above subjects are reviewed in CPR, a board review program.

School of Graduate and Postdoctoral Studies

  • Basics of Structural Biology, molecular recognition and enzyme action in Molecular and Cell Biology II GIGP502
  • Fluorescence and Isothermal Calorimetry in Physical Biochemistry GBCH544
  • Phosphoryl transfer reactions catalyzed by enzymes and ribozymes in Enzyme Structure and Mechanism GBCH543