Abstract Title

Investigation of folding thermodynamics and kinetics of cobalamin riboswitch

Abstract

Cobalamin or vitamin B12 is a water soluble vitamin that aids in the metabolism of bacteria. Cobalamin riboswitch is found at the 5’-UTR of the btuB mRNA that expresses cobalamin related proteins. Upon binding of Ado-cobalamin (Ado-Cbl), the respective riboswitch undergoes conformational rearrangement to sequester the ribosome binding site of btuB mRNA. These conformational changes in mRNA result in translation inhibition of Ado-Cbl related proteins. Discovery of molecules that target Ado-Cbl riboswitch RNA and undergo similar conformational changes upon its binding can be a successful strategy to develop new antibiotics that targets B12 biosynthesis. My current research is focused on determining the thermodynamic and kinetic changes that are associated with riboswitch folding and regulation using various spectroscopic methods. These studies will enable us to clearly understand the energetics of Ado-Cbl riboswitch function.

Modified Abstract

Cobalamin or vitamin B12 aids in the metabolism of bacteria. Cobalamin riboswitch is found at the 5’-UTR of the btuB mRNA that expresses cobalamin related proteins. Upon binding of Ado-cobalamin (Ado-Cbl), the respective riboswitch undergoes conformational rearrangement to sequester the ribosome binding site of btuB mRNA. These conformational changes in mRNA result in translation inhibition of Ado-Cbl related proteins. Discovery of molecules that target Ado-Cbl riboswitch RNA and undergo similar conformational changes upon its binding can be a successful strategy to develop new antibiotics that targets B12 biosynthesis. My current research focuses on determining the thermodynamic and kinetic changes that are associated with riboswitch folding and regulation using various spectroscopic methods. These studies will enable us to clearly understand the energetics of Ado-Cbl riboswitch function.

Research Category

Physics/Chemisty/Liquid Crystal

Primary Author's Major

Biology

Mentor #1 Information

Dr. Sanjaya Abeysirigunawardena

Presentation Format

Poster

Start Date

March 2016

Investigation of folding thermodynamics and kinetics of cobalamin riboswitch.docx (12 kB)
Investigation of folding thermodynamics and kinetics of cobalamin riboswitch

Research Area

Biochemistry | Biochemistry, Biophysics, and Structural Biology | Life Sciences

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Mar 15th, 1:00 PM

Investigation of folding thermodynamics and kinetics of cobalamin riboswitch

Cobalamin or vitamin B12 is a water soluble vitamin that aids in the metabolism of bacteria. Cobalamin riboswitch is found at the 5’-UTR of the btuB mRNA that expresses cobalamin related proteins. Upon binding of Ado-cobalamin (Ado-Cbl), the respective riboswitch undergoes conformational rearrangement to sequester the ribosome binding site of btuB mRNA. These conformational changes in mRNA result in translation inhibition of Ado-Cbl related proteins. Discovery of molecules that target Ado-Cbl riboswitch RNA and undergo similar conformational changes upon its binding can be a successful strategy to develop new antibiotics that targets B12 biosynthesis. My current research is focused on determining the thermodynamic and kinetic changes that are associated with riboswitch folding and regulation using various spectroscopic methods. These studies will enable us to clearly understand the energetics of Ado-Cbl riboswitch function.