Poster abstracts
Poster number 146 submitted by Minhchau To
S4-like domain regulates binding of RsuA to 16S rRNA
Minhchau To (Chemistry & Biochemistry, Kent State University), Kumudie Jayalath (Chemistry & Biochemistry, Kent State University), Sanjaya Abeysirigunawardena (Chemistry & Biochemistry, Kent State University)
Abstract:
The Ribosomes are ribonucleoprotein complexes that are involved in protein biosynthesis in all living organisms. Bacterial ribosome biogenesis is a complex process that is dependent on the integration of several cellular events, such as ribosomal RNA transcription, ribosome assembly, RNA processing and post-transcriptional and post-translational modification of ribosomal RNA and proteins, respectively. Even though the ribosome assembly is well studied, the impact of post-transcriptional rRNA modification enzymes and their respective modifications on ribosomal assembly is not completely understood. Pseudouridine synthase, RsuA, is responsible for the formation of pseudouridine at position 516. Protein RsuA is composed of two domains including the C-terminal catalytic domain and the N-terminal S4-like domain. My study focuses on understanding the importance of the N-terminal S4 like domain for RsuA binding and its function. Our filter binding assays show decrease in binding affinity in the absence of the S4-like domain. However, unlike the full length protein, the truncated RsuA protein is capable of binding to 16S rRNA at much higher protein concentrations suggesting an auto inhibitory role for the S4-like domain.
Keywords: Ribosome biogenesis, RNA modification enzyme, Pseudouridine