Kurt Fredrick
Contact Information
- fredrick.5@osu.edu
- Phone
- (614) 292-6679
- Office
- 286 Aronoff Laboratory
Areas of Expertise
- Protein Synthesis
- Ribosome Assembly and Function
- Gene Regulation
- Antibiotic Mode of Action
Education
- B.A. Gustavus Adolphus College, 1992
- Ph.D. Cornell University, 1997
- Postdoc, UC-Santa Cruz, 1997-2003
Affiliations
- Center for RNA Biology
- Ohio State Biochemistry Program
- Cellular, Molecular, and Biochemical Sciences Program
Awards
- Fellow, American Association for the Advancement of Science
- Fellow, American Academy of Microbiology
Research Interests
Protein synthesis (or translation) is catalyzed by ribosomes in all cells. Ribosomes are large (~2.5 MDa), RNA-based, two-subunit machines containing several RNA molecules and ~50 distinct polypeptides. Proteins termed translation factors facilitate the initiation, elongation, termination, and recycling stages of translation. Dozens of other proteins interact with ribosomes in the cell to monitor, modulate, and/or regulate the translation process.
We use a combination of genetic, molecular, and biochemical methods to study ribosome assembly and function in bacteria. Questions under investigation in the laboratory include: (1) How does the bS21-status of ribosomes regulate translation in various lineages? (2) How does 16S rRNA heterogeneity impact cell physiology? (3) How do mechanisms of initiation compare in different phyla? (4) What roles do nonessential ribosome-associated GTPases play in the cell? (5) How do elements of precursor rRNA contribute to subunit assembly?
Some Recent Publications:
Naeem, F.M., Roy, B., Arpin, D., McNutt, Z.A., Moon, K-M., Gemler, B.T., Bundschuh, R., Foster, L.J., Ortega, J., and Fredrick, K. 2026. Role of the anti-Shine-Dalgarno sequence of 16S rRNA in Flavobacterium johnsoniae. Nucleic Acids Res. 54, gkag239
Arpin, D., Roy, B., Naeem, F.M., Fredrick, K.*, and Ortega, J.* 2026. Structure of a specialized 70S initiation complex. Nucleic Acids Res. 54, gkag094. (*co-corresponding authors)
Alom, M.S., Arpin, D., Zhu, H., Hay, B.N., Foster, L.J., Ortega, J., and Fredrick, K. 2025. Protein bL38 facilitates incorporation of uL6 during assembly of the 50S subunit in Flavobacterium johnsoniae. Nucleic Acids Res. 53, gkaf120.
Fakhretaha Aval, S., Seffouh, A., Moon, K-M., Foster, L.J., Ortega, J., and Fredrick, K. 2025. Role of the sarcin-ricin loop of 23S rRNA in biogenesis of the 50S subunit. RNA 31, 585-599.
Gemler, B.T., Warner, B.R., Bundschuh, R. and Fredrick, K. 2024. Identification of leader-trailer helices of precursor ribosomal RNA in all phyla of bacteria and archaea. RNA 30, 1264-1276.
Warner, B.R. and Fredrick, K. 2024. Contribution of an alternative 16S rRNA helix to biogenesis of the 30S subunit of the ribosome. RNA 30, 770-778.
Naeem, F.M., Gemler, B.T., McNutt, Z.A., Bundschuh, R. and Fredrick, K. 2024. Analysis of programmed frameshifting during translation of prfB in Flavobacterium johnsoniae. RNA 30, 136-148.
Warner, B.R., Bundschuh, R. and Fredrick, K. 2023. Roles of the leader-trailer helix and antitermination complex in biogenesis of the 30S ribosomal subunit. Nucleic Acids Res. 51, 5242-5454.
McNutt, Z.A., Roy, B., Gemler, B.T., Shatoff, E.A., Moon, K-M., Foster, L.J., Bundschuh, R. and Fredrick, K. 2023. Ribosomes lacking bS21 gain function to regulate protein synthesis in Flavobacterium johnsoniae. Nucleic Acids Res. 51, 1927-1942.
McNutt, Z.A., Gandhi, M.D., Shatoff, E.A., Roy, B., Devaraj, A., Bundschuh, R. and Fredrick, K. 2021. Comparative analysis of anti-Shine-Dalgarno function in Flavobacterium johnsoniae and Escherichia coli. Front. Mol. Biosci. 8, 787388.
Shatoff, E.A., Gemler, B.T., Bundschuh, R. and Fredrick, K. 2021. Maturation of 23S rRNA includes removal of helix H1 in many bacteria. RNA Biol. 18(sup2), 856-865.
Jha, V., Roy, B., Jahagirdar, D., McNutt, Z.A., Shatoff, E.A., Boleratz, B.L., Watkins, D.E., Bundschuh, R., Basu, K., Ortega, J. and Fredrick, K. 2021. Structural basis of sequestration of the Anti-Shine-Dalgarno sequence in the Bacteroidetes ribosome. Nucleic Acids Res. 49, 547-567.
All publications:
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