Abstract

The Ribosome is a ribonucleoprotein molecular machine that biosynthesize protein in cells. Accurate biogenesis of a ribosome is critical for cell survival. Previous studies on ribosomal assembly suggest that post-transcriptional modification steps are important for accurate biogenesis of ribosomes. However, the mechanism of how these modifications influence ribosomal biogenesis is yet to be known. Protein RsmC is an enzyme that post-transcriptionally methylates G1207 of 16S ribosomal RNA. Previous studies have shown that RsmC reacts optimally at 0.9 mM MgCl2; whereas, at both 6 mM MgCl2 methylation was decreased by 3-fold. These results suggest that RsmC may be interacting with RNA co-transcriptionally and may also assist in RNA annealing. To test this hypothesis, I carried out Fluorescence-based native gel electrophoresis experiments to determine RNA annealing thermodynamics in the presence and absence of protein RsmC under various magnesium ion concentrations. My data suggests that RsmC stabilizes the RNA duplex at 4 mM Magnesium ion concentrations. This result emphasizes that RsmC enzyme aids ribosome biogenesis by preventing miss folding of ribosomal RNA during ribosome biogenesis.

Modified Abstract

Accurate biogenesis of the ribosome is critical for cell survival. Previous studies on ribosomal assembly suggest that post-transcriptional modification steps are important for accurate biogenesis of ribosome. Protein RsmC is an enzyme that post-transcriptionally methylates G1207 of 16S ribosomal RNA. Previous studies suggest that RsmC may assist in annealing of two RNA strands. To test this hypothesis, I carried out Fluorescence-based native gel electrophoresis experiments to determine RNA annealing thermodynamics in the presence and absence of protein RsmC under various magnesium ion concentrations. My data suggest that RsmC stabilize RNA duplex at 4 mM Magnesium ion concentration. This result shows that RsmC enzyme will prevent miss folding of ribosomal RNA during ribosome biogenesis.

Research Category

Physics/Chemisty/Liquid Crystal

Primary Author's Major

Biology

Mentor #1 Information

Mr. Keshav GC

Mentor #2 Information

Dr. Sanjaya Abeysirigunawardena

Presentation Format

Poster

Start Date

21-3-2017 1:00 PM

Research Area

Amino Acids, Peptides, and Proteins | Biological Factors

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Mar 21st, 1:00 PM

RsmC Stabilizes the Formation of Helix 34 of 16S Ribosomal RNA

The Ribosome is a ribonucleoprotein molecular machine that biosynthesize protein in cells. Accurate biogenesis of a ribosome is critical for cell survival. Previous studies on ribosomal assembly suggest that post-transcriptional modification steps are important for accurate biogenesis of ribosomes. However, the mechanism of how these modifications influence ribosomal biogenesis is yet to be known. Protein RsmC is an enzyme that post-transcriptionally methylates G1207 of 16S ribosomal RNA. Previous studies have shown that RsmC reacts optimally at 0.9 mM MgCl2; whereas, at both 6 mM MgCl2 methylation was decreased by 3-fold. These results suggest that RsmC may be interacting with RNA co-transcriptionally and may also assist in RNA annealing. To test this hypothesis, I carried out Fluorescence-based native gel electrophoresis experiments to determine RNA annealing thermodynamics in the presence and absence of protein RsmC under various magnesium ion concentrations. My data suggests that RsmC stabilizes the RNA duplex at 4 mM Magnesium ion concentrations. This result emphasizes that RsmC enzyme aids ribosome biogenesis by preventing miss folding of ribosomal RNA during ribosome biogenesis.