Poster abstracts
Poster number 43 submitted by Caitlin Hawkins
Characterization of minimal binding site of modification enzyme RsmG
Caitlin Hawkins (Department of Chemistry and Biochemistry - Kent State University), Kumudie Jayalath (Department of Chemistry and Biochemistry - Kent State University), Sanjaya Abeysirigunawardena (Department of Chemistry and Biochemistry - Kent State University)
Abstract:
Ribosomes are the molecular machines that carry out protein biosynthesis in all living organisms. They are composed of three different ribosomal RNAs and more than 50 ribosomal proteins. The thermodynamics and kinetics of in vitro ribosomal assembly have been studied extensively. However, during in vivo ribosome biogenesis, ribosome assembly occurs concurrently with transcription, folding, post-transcriptional modification, and processing of rRNA. Unfortunately, the effects post-transcriptional RNA modification enzymes on ribosomal assembly are understudied. My project in Abey lab is to investigate how RNA modification enzyme RsmG influences 30S bacterial ribosome assembly. I have developed a FRET-based assay to monitor the binding of RsmG to ribosomal RNA, which will allow us to determine the binding affinity of RsmG to RNA, and thus calculate thermodynamic cooperativity between the RsmG enzyme and ribosomal proteins. Our findings give us more insight into how modification enzymes modulate the hierarchy of protein addition during ribosome biogenesis.
Keywords: ribosome assembly, RNA-protein interactions, nucleotide modifications