N-terminal domain of rRNA methyltransferase enzyme RsmC is important for its binding to RNA and RNA chaperone activity
Author(s)
Abstract

Ribosomal RNA modification enzyme, Ribosomal small subunit methyltransferase C (RsmC) plays a dual role of methylating the exocyclic amine of G1207 of 16S ribosomal RNA and functioning as an RNA chaperone. RsmC carries Methyltransferase active C-terminal domain and catalytically inert N-terminal domain. This project is focused on identifying the importance of the N-terminal domain and its role in the RNA chaperone activity. Site-directed mutagenesis was used to delete the C-terminal domain. Mutant proteins were purified
using affinity chromatography. Mutant protein was found to have a lower affinity to both strands of helix 34 that carries G1207. Similarly, the RsmC deletion mutant influenced the annealing of helix 34 strands. These observations reveal the molecular mechanism of RNA chaperone activity of RsmC and its role in ribosome biogenesis.
Format
Conference Proceeding
Date
2021-04-20
Contributor(s)
Faculty Mentor
Sanjaya Abeysirigunawardena
Rights
http://rightsstatements.org/vocab/InC/1.0/
Comments

Poster

Symposium brochure page 20
Permalink https://oaks.kent.edu/ugresearch/2021-kent-state-university-undergraduate-symposium-research-scholarship-and-creative-6/n
Kshetri, M., & GC, K. (2021). N-terminal domain of rRNA methyltransferase enzyme RsmC is important for its binding to RNA and RNA chaperone activity (1–). https://oaks.kent.edu/node/16589
Kshetri, Man, and Keshav GC. 2021. “N-Terminal Domain of RRNA Methyltransferase Enzyme RsmC Is Important for Its Binding to RNA and RNA Chaperone Activity”. https://oaks.kent.edu/node/16589.
Kshetri, Man, and Keshav GC. N-Terminal Domain of RRNA Methyltransferase Enzyme RsmC Is Important for Its Binding to RNA and RNA Chaperone Activity. 20 Apr. 2021, https://oaks.kent.edu/node/16589.