Investigating the role of RsmC C-terminal domain in RNA binding
Author(s)
  • Minhchau To Sophomore, Chemistry (Biochemistry–Pre-Medicine/Pre-Osteopathy/Pre-Dentistry)
  • Man Kshetri Junior, Biotechnology
  • Keshav GC Graduate Student , Chemistry
Abstract
Ribosomes are the large ribonucleoprotein complexes that are responsible for protein biosynthesis in all organisms. The ribosome’s accuracy regarding its function is heavily controlled by its structural integrity. Ribosomal RNA modifications can influence nearby structures which can then influence the functional efficiency of the ribosome. The focus of the Abey Lab is to understand the ability of nucleotide modifications and their respective modification enzymes in the process of biogenesis of ribosomes. The rRNA nucleotide modification enzyme RsmC is important for the m2G modification at position 1207 in the 16S rRNA. Protein RsmC has an N-terminal domain that functions as the catalytic domain, which is connected to the C-terminal domain through a flexible linker. We hypothesize that the C-terminal domain is important for its binding. We performed site-directed mutagenesis to delete the entire C-terminal domain. We carried out filter binding assays with the mutant and the wildtype protein to determine if C-terminal domain plays a role in binding of RNA.
Format
Conference Proceeding
Contributor(s)
Faculty Mentor
Sanjaya Abeysirigunawardena
Modified Abstract

Ribosomes are large ribonucleoprotein complexes that are responsible for protein biosynthesis in all organisms. Ribosomal RNA modifications can influence the functional efficiency of ribosomes. The focus of the Abey Lab is to understand the ability of nucleotide modifications and their respective modification enzymes in ribosomal biogenesis The rRNA nucleotide modification enzyme RsmC is important for the m2G modification at position 1207 in the 16S rRNA. Protein RsmC has an N-terminal domain that functions as the catalytic domain, connected to a C-terminal domain. We hypothesize that the C-terminal domain is important for its binding and used site-directed mutagenesis to delete it. We carried out filter binding assays with the mutant and the wildtype protein to determine if C-terminal domain plays a role in binding of RNA.
Permalink https://oaks.kent.edu/ugresearch/2020/physicschemistryliquid-crystal/investigating-role-rsmc-c-terminal-domain-rna
To, M., Kshetri, M., & GC, K. (n.d.). Investigating the role of RsmC C-terminal domain in RNA binding (1–). https://oaks.kent.edu/node/10283
To, Minhchau, Man Kshetri, and Keshav GC. n.d. “Investigating the Role of RsmC C-Terminal Domain in RNA Binding”. https://oaks.kent.edu/node/10283.
To, Minhchau, et al. Investigating the Role of RsmC C-Terminal Domain in RNA Binding. https://oaks.kent.edu/node/10283.