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. During ribosome biogenesis, in vivo ribosome assembly occurs concurrently with transcription, folding, post-transcriptional modifications 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 an assay to monitor 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 RsmG enzyme and ribosomal proteins. Our findings give us more insight to how modification enzymes modulate the hierarchy of protein addition during ribosome biogenesis.

Modified 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. My project in Abey lab is to investigate how RNA modification enzyme RsmG influences ribosomal proteins binding to 16S ribosomal RNA. To achieve this goal, I have developed an assay to monitor 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 RsmG enzyme and ribosomal proteins. Our findings give us more insight to how modification enzymes modulate the hierarchy of protein addition during ribosome biogenesis.

Research Category

Physics/Chemisty/Liquid Crystal

Author Information

Caitlin HawkinsFollow

Primary Author's Major

Biochemistry

Mentor #1 Information

Dr. Sanjaya Abeysirigunawardena

Presentation Format

Poster

Start Date

21-3-2017 1:00 PM

Research Area

Biochemistry, Biophysics, and Structural Biology

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Mar 21st, 1:00 PM

Development of FRET-Based Assay to Observe Binding of RNA Modification Enzyme RsmG to 16S Ribosomal RNA

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. During ribosome biogenesis, in vivo ribosome assembly occurs concurrently with transcription, folding, post-transcriptional modifications 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 an assay to monitor 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 RsmG enzyme and ribosomal proteins. Our findings give us more insight to how modification enzymes modulate the hierarchy of protein addition during ribosome biogenesis.