Date of Award

1-1-2020

Language

English

Document Type

Master's Thesis

Degree Name

Master of Science (MS)

College/School/Department

Department of Chemistry

Content Description

1 online resource (iv, 59 pages) : color illustrations.

Dissertation/Thesis Chair

Alexander Shekhtman

Committee Members

Daniele Fabris

Keywords

Nuclear magnetic resonance spectroscopy, Ribosomes, Enzymes, Cells, Glycolysis

Subject Categories

Chemistry

Abstract

Recent research has been performed to better understand what implications ribosome-mediated quinary interactions have on cellular growth. These studies demonstrated that ribosomal binding to enzymes, and their cofactors, can cause significant changes in their enzymatic activity leading to a proposal that ribosome surfaces play a greater regulatory in cellular growth than thought of in the past. To widen the scope of investigations performed on these ribosomal-mediated quinary interactions, the regulatory enzymes associated in glycolysis (hexokinase, phosphofructokinase, and pyruvate kinase) were titrated into a solution of 70S E. coli ribosome and analyzed via 1H-15N-HSQC NMR. The perturbations of the peaks associated with a ribosome-enzyme titration when compared to the free ribosome state indicated a ribosome-glycolytic enzyme bound state. When compared to the perturbations observed for thiostrepton-ribosome bound states, it has been determined that there is binding occurring in the L11 arm region of the 70S ribosome rRNA backbone with the three regulatory glycolytic enzymes. This data suggests that the metabolic control of glycolysis in the cell could be affected by the ribosome concentration in the cell, leading to another level of cellular growth regulations associated with ribosome-mediated quinary interactions.

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