Author

Mariam Bhatti

Bound Volume Number

Volume II

Document 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.

Creative Commons License

Creative Commons Attribution 3.0 License
This work is licensed under a Creative Commons Attribution 3.0 License.

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