Bound Volume Number
Volume II
Degree Type
Honors Capstone Project
Date of Submission
Spring 5-2016
Capstone Advisor
Tom Duncan
Capstone Major
Biology
Capstone College
Arts and Science
Audio/Visual Component
no
Keywords
Adenosine triphosphate, phosphoanhydride
Capstone Prize Winner
no
Won Capstone Funding
yes
Honors Categories
Sciences and Engineering
Subject Categories
Biology
Abstract
Adenosine triphosphate (ATP) contains energy-rich phosphoanhydride bonds that provide the energy needed for many cellular processes. F-type ATP synthase is found in bacteria, chloroplasts, and mitochondria, having a conserved function to catalyze the synthesis and hydrolysis of ATP. ATP synthase is a membrane bound rotary motor enzyme, with coupled rotation between it’s two distinct complexes Fo and F1. In bacteria and chloroplasts, the ε-subunit’s C-terminal Domain (εCTD) has a distinct regulatory function that is absent in mitochondria. Determining the inhibitory interactions of ε is important in understanding it’s physiological functions and for potential targeting of ε’s bacteria-specific inhibition for development of new antibiotics. Guided by a high-resolution structure of ε inhibition catalytic complex, in this study I use site-specific mutagenesis of the εCTD in Escherichia coli (E. coli) to investigate interactions and make mutations at regions important for ε inhibition. I then analyze the effects of these mutants through phenotypic growth and ATP hydrolysis assays.
Recommended Citation
Bhatti, Mariam, "Structure-Guided Site-Directed Mutagenesis of the Bacterial ATP Synthase’s Epsilon Subunit" (2016). Honors Capstone Projects - All. 966.
https://surface.syr.edu/honors_capstone/966
Creative Commons License
This work is licensed under a Creative Commons Attribution 3.0 License.
