Blaine H.M. Mooers, PhD

Associate Professor
Director of the Laboratory of Biomolecular Structure and Function

RNA and protein structural biologist using crystallography and small angle scattering. 

Contact Information:

Office: BRC 468

Phone: (405) 271-8300

Mailing Address:

University of Oklahoma Health Sciences Center

975 N.E. 10th, BRC468
Oklahoma City, OK  73104


PhD, Oregon State University, 1997

Post-doc, HHMI/Univeristy of Oregon 2003

Research Associate, University of Oregon 2006

Research Interests:

Structural biology of messenger RNA editing in the mitochondria of trypanosome


Uridine (U) insertion/deletion editing in trypanosomes is an extensive post-transcriptional process that corrects the coding sequence of most mitochondrial mRNAs.  This editing is required for the subsequent expression of several mitochondrial proteins.  The number of Us that are inserted far exceeds that number that are deleted; there is a net increase in the number of codons after editing.  An enzyme cascade does the editing in the mitochondrion.  The editing reactions are directed by a number of different guide RNAs.  Each guide RNA has the sequence complement of a fragment of the final edited mRNA sequence. Consequently, much of the genetic information for the final RNA transcript comes from both its corresponding gene and the genes for the set of guide RNAs that direct its editing.  In other words, the genetic information flows from DNA to RNA along multiple parallel pathways.  This is an interesting variation of the central paradigm of molecular biology that information flows along one pathway from DNA→RNA→protein.  The evolutionary basis for such a complex and expensive system of information flow is still unclear. 

Our goal is to obtain a rigorous description of the structural biology of this type of RNA editing to improve our understanding of its evolutionary basis, clarify the relationship between this type of RNA editing and other types of RNA editing, and to provide a structural basis of the design of better drugs to fight infections with trypanosomes which threaten 600 million people worldwide. 

Selected Publications:

(*corresponding author, pdb codes from structures determined in my lab or by me):  

  • Terzyan SS, Shen T, Liu X, Huang Q, Teng P, Zhou M, Hilberg F, Cai J, ^Mooers, BHM, ^Wu J (2019). Structural basis of resistance of mutant RET protein tyrosine kinase to its inhibitors nintedanib and vandetanib. J Biol Chem .  294(27):10428-37.jbc.RA119.007682. doi:Epub 2019/05/24. PubMed PMID: 31118272. doi:10.1074/jbc.RA119.007682. ^Co-correpsonding authors. PDB IDs: 6NEC, 6NAJ, and 6NE7.
  • Kumar V, Doharey PK, Gulati S, Meehan J, Martinez MG, Hughes K, ^Mooers BHM, ^Cruz-Reyes J.  (2019) Protein features for assembly of the RNA editing helicase 2 subcomplex (REH2C) in Trypanosome holo-editosomes. PLOS ONE 14(4):e0211525. doi: 10.1371/journal.pone.0211525. ^Co-correpsonding authors.
  • Cruz‐Reyes, J., Mooers, B. H., Doharey, P. K., Meehan, J., & Gulati, S. (2018)  Dynamic RNA holo‐editosomes with subcomplex variants: Insights into the control of trypanosome editing. Wiley Interdisciplinary Reviews: RNA, e1502. PMID: 30101566.
  • Liu, X., Shen, T., Mooers, B. H., Hilberg, F., & Wu, J. (2018)  Drug resistance profiles of mutations in the RET kinase domain. British Journal of Pharmacology 175:3504-3515. doi: 10.1111/bph.14395. PMID: 29908090.
  • Cruz-Reyes, J., Mooers, B. H., Kumar, V., Doharey, P. K., Meehan, J., & Chaparro, L. (2018)  Control Mechanisms of the Holo-Editosome in Trypanosomes. In RNA Metabolism in Mitochondria (pp. 125-144). Springer, Cham.
  • Mooers, B. H. M.* (2016)  Simplifying and enhancing the use of PyMOL with horizontal scripts. Protein Sci. 25(10):1873-82. PMID: 27488983
  • Cruz-Reyes, J.,  Mooers, B.H.M.,  Abu-Adas, Z., Kumar, V., & Gulati, S. (2016)  DEAH-RHA helicase• Znf cofactor systems in kinetoplastid RNA editing and evolutionarily distant RNA processes. RNA & Disease 3. pii: e1336.
  • Mooers, B. H. M.* (2016) Direct-methods structure determination of a trypanosome RNA-editing substrate fragment with translational pseudosymmetry. Acta Cryst. D72, 477-487. doi: 10.1107/S2059798316001224. 5AD6.
  • Kumar, V., Madina, B.R., Gulati, S., Vashishti, A.A., Kanyumbu, C., Pieters, B., Shakir, A., Wohlschlegel, J.A., Read, L.K., Mooers, B.H.M. & Cruz-Reyes, J. (2016) REH2C helicase and GRBC subcomplexes may base pair through mRNA and small guide RNA in kinetoplastid editosomes.  J. Biol. Chem. 291,5753-64. doi: 10.1074/jbc.M115.708164
  • Gu, X., Mooers, B.H.^, Thomas, L.M., Malone, J., Harris, S.M., and Schroeder, S.J.^ (2015) Structures and energetics of four adjacent G·U pairs that stabilize an RNA helix. J. Phys. Chem. B.  119,13252-61.  doi: 10.1021/acs.jpcb.5b06970. PMID: 26425937. PDB-code: 4PCO. ^Co-corresponding authors.
  • Terzyan, S.S., Burgett, A.W., Heroux, A., Smith, C.A., Mooers B.H., and Hanigan, M.H. (2015) Human Gamma-glutamyl transpeptidase 1: structures of the free enzyme, inhibitor-bound tetrahedral transition states and glutamate bound enzyme reveal novel movement within the active site during catalysis. J Biol Chem. 290,17576-86. doi: 10.1074/jbc.M115.659680.  PMID: 26013825.
  • Madina, B.R., Kumar, V., Mooers, B.H.M., and Cruz-Reyes*, J. (2015) Native variants of the MRB1 complex exhibit specialized functions in kinetoplastid RNA editing. PLoS One 10(4):e0123441. doi: 10.1371/journal.pone.0123441. PMID: 25928631.
  • Mooers, B.H.M.* (2015)  RNA Fusions in crystallographic studies of double-stranded RNA from trypanosome RNA editing. Methods in Mol. Biol. 1240, 191-216. doi:10.1007/978-1-4939-1896-6_14. PMID: 25352146.
  • Criswell, A. and Mooers, B.H.M.* (2015)  Structural studies of a double-stranded RNA trypanosome RNA editing by small-angle X-ray scattering. Methods in Mol. Biol. 1240, 191-216. doi: 10.1007/978-1-4939-1896-6_13. PMID: 25352145.
  • Madina, B.R., Kumar, V., Metz, R., Mooers, B.H.M. Bundschuh, R., and Cruz-Reyes, J. (2014)  Native mitochondrial RNA-binding complexes in kinetoplastid RNA editing differ in guide RNA composition. RNA 20, 1142-52. doi:10.1261/rna.044495.114. PMID: 24865612.
  • Ding, J., Mooers, B.H.M., Zhang, Z., Kale, J., Falcone, D., McNichol, J., Huang, B., Zhang, X.C., Xing, C., Andrews, D.W., and Lin, J. (2014)  After embedding in membranes antiapoptotic Bcl-XL protein binds both Bcl-2 homology region 3 and helix 1 of proapoptotic Bax protein to inhibit apoptotic mitochondrial permeabilization. J. Biol. Chem. 289, 11873-96. doi:10.1074/jbc.M114.552562.  PMID: 24616095.
  • Sheikh, M.O., Schafer, C.M., Powell, J.T., Rodgers, K.K., Mooers, B.H.M., and West, C.M. (2014) Glycosylation of Skp1 affects its conformation and promotes binding to a model F-box protein. Biochemistry 53, 1657-69. doi:10.1021/bi401707y.  PMID: 24506136.
  •  West, M.B., Chen, Y., Wickham, S., Heroux, A., Cahill, K., Hanigan, M.H., and Mooers, B.H.M.* (2013) Novel insights into eukaryotic γ-glutamyl transpeptidase 1 from the crystal structure of the glutamate-bound human enzyme. J. Biol. Chem. 288, 31902-31913. doi:10.1074/jbc.M113.498139. PMID: 24047895. PDB-codes: ‎4GDX4GG2
  •  Mooers, B.H.M.* (2013) Structural studies of U-insertion/deletion RNA editing in trypanosomes. In Maas, S. (ed) RNA Editing: Current Research and Future Trends. Caister Academic Press, Norfolk. p. 91-124.
  • Venkatramani, L., Johnson, E.S., Kolavi, G., Air, G.M., Brouillette W.J.*, Mooers B.H.M.* (2012) Crystal structure of a new benzoic acid inhibitor of influenza neuramidase bound with a new tilt induced by overpacking sub-site C6. BMC Struct Biol.12:7. doi: 10.1186/1472-6807-12-7.  PMID: 22559154. PDB-Code: 4DGR.

  • Mooers, B.H.M.* & Singh, A. (2011)  The crystal structure of an oligo(U):pre-mRNA duplex from a trypanosome RNA editing substrate. RNA 17, 1870-83.  doi: 10.1261/rna.2880311.  PMID; 21878548. PDB-Code: 3ND33ND4.

  • Mooers, B.H.M., Baase, W.A., Wray, J.W., & Matthews, B.W.  (2009)  Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme.  Protein Sci. 18, 871-880.  PDB-Codes: 3C7Y3C8R3C7W3C7Z3C803C81, 3C823C8Q3C833C8R3C8S3CDO3CDQ3CDR3CDT3CDV3FI5.

  • Mooers, B.H.M., Tronrud, E.D., & Matthews, B.W. (2009)  Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 --> His. Protein Sci. 18, 863-870. doi: 10.1002/pro.93. PMID:19384984.  PDB-Codes: 3F8V3F9L3FA03FAD

  • Mooers, B.H.M.* (2008)  Crystallographic studies of DNA and RNA. Methods 47, 168-176. doi: 10.1016/j.ymeth.2008.09.006.  PMID: 18848992.

  • Mooers, B.H.M.*  & Matthews, B. W.  (2006)  Extension to 2268 atoms of direct methods in the ab initio determination of the unknown structure of bacteriophage P22 lysozyme. Acta Cryst. D 62, 165-76.  *Corresponding author.doi:10.1107/S0907444905037212.  PMID: 16421448. PDB-Codes: 2ANX2ANV

  • Mooers,B.H.M., Logue, J.S. & Berglund, J.A. (2005)  The structural basis of myotonic dystrophy from the crystal structure of CUG repeats. Proc. Nat. Acad. Sci., USA 102, 16626-16631. 
     doi: 10.1073/pnas.0505873102.  PMID: 16269545.
  • Mooers, B.H.M. & Matthews, B.W. (2004) Use of an ion binding site to by-pass the 1000 atom limit to ab initio structure determination by direct methods. Acta Cryst. D 60, 1726-1737. doi:10.1107/S0907444904017020. PMID: 15388918.  PDB-Codes: 1SWZ1SX71SX2, and 1SWY

  • Mooers, B.H.M., Datta, D., Zollars, E., Mayo, S.L., & Matthews, B. W. (2003) Repacking the core of T4 lysozyme by automated design. J. Mol. Biol.  332, 741-756. PDB-Codes: 1PQM1PQO1PQK1PQJ1PQI1PQD1P7S1P461P6Y1P641P461P3N1P371P361P2R1P2L

Link to full publication list >