Katie Berry

Clare Boothe Luce Assistant Professor of Biochemistry
Biochemistry, RNA-protein interactions, gene regulation

Katie Berry received her Ph.D. at University of California, Berkeley, where she used biochemical and biophysical techniques to study the mechanism of action of a non-coding RNA that Hepatitis C virus uses to appropriate human ribosomes during infection.During her postdoctoral training, Berry learned tools of bacterial molecular genetics to ask questions about the mechanism of gene regulation, and the role non-coding RNAs play inside of living bacterial cells.At Mount Holyoke, Berry’s lab combines these interests and makes use of both in vitro and in vivo approaches.

RNA-protein interactions are critical for gene regulation and the adaptation to stress in all organisms.Berry’s research addresses the molecular mechanisms of how small (s)RNAs in bacteria collaborate with proteins such as Hfq to regulate messenger RNA translation and stability.Berry has recently developed an in vivo assay to harness the power of molecular genetics to discover and characterize RNA-protein interactions inside of E. coli cells. She has used this assay to learn more about how the E. coli RNA chaperone protein Hfq binds to its regulatory sRNAs. Students in her lab will be able to adapt this assay to new interactions to explore the diversity of how small RNAs interact with their protein collaborators across bacteria that cause human diseases, and quantitatively dissect these interactions using complementary biochemical tools.

Berry teaches in Biochemistry and introductory Chemistry.

Recent Publications

Stein, EM, Kwiatkowska, J, Basczok, MM, Gravel, CM [MHC '20], Berry, KE, & Olejniczak, M. 2020. Determinants of RNA recognition by the FinO domain of the Escherichia coli ProQ protein. Nucleic Acids Research, 48(13): 7502-19. https://doi.org/10.1093/nar/gkaa497

Pandey, S. [MHC '19], Gravel, C.M. [MHC '20], Stockert, O.M. [MHC '21], Wang, C.D. [MHC '19], Hegner, C.L. [MHC '19], LeBlanc, H. [MHC '20] & Berry, K.E., Genetic identification of the functional surface for RNA binding by Escherichia coli ProQ. Nucleic Acids Research, gkaa144, DOI: 10.1093/nar/gkaa144. (March 14, 2020)

Berry K.E., Waghray S.*, Mortimer S.A., Bai Y., Doudna J.A. (2011) Crystal structure of the HCV IRES central domain reveals strategy for start-codon positioning. Structure, 19, 1456-66. (* indicates undergraduate mentee)

Berry K.E., Peng B., Koditek D., Beeman D., Pagratis N., Perry J.K., Parrish J., Zhong W., Doudna J.A., Shih I-h. (2011) Optimized high-throughput screen for Hepatitis C virus translation inhibitors. J Biomol Screen, 16, 211-20.

Berry K.E., Waghray S.*, Doudna J.A. (2010) The HCV IRES pseudoknot positions the initiation codon on the 40S ribosomal subunit. RNA, 16, 1559-69.  (* indicates undergraduate mentee)