Graduate Studies, UNL

 

Dissertations and Doctoral Documents, University of Nebraska-Lincoln, 2023–

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First Advisor

Rebecca Roston

Degree Name

Doctor of Philosophy (Ph.D.)

Committee Members

Christian Elowsky, Ed Cahoon, Oleh Khalimonchuk, Toshi Obata

Department

Biochemistry

Date of this Version

4-21-2026

Document Type

Dissertation

Citation

A dissertation presented to the faculty of the Graduate College at the University of Nebraska in partial fulfillment of requirements for the degree Doctor of Philosophy

Major: Biochemistry

Under the supervision of Professor Rebecca Roston

Lincoln, Nebraska, May 2026

Comments

Copyright 2026, Cailin Smith. Used by permission

Abstract

Chloroplasts are green, photosynthetically active organelles ubiquitous to the plant kingdom. Owing to their cyanobacterial origin, chloroplasts consist of three membranes: the outer envelope, the inner envelope, and the thylakoid, the latter of which is the site of the light-dependent reactions of photosynthesis. Not only do the lipids that make up these membranes delineate aqueous compartments, but they also respond dynamically to developmental and environmental cues, constitute the matrix that scaffolds protein machinery, and even serve as functional components of some proteinaceous complexes. However, while lipids are of vital importance to the structure and function of the chloroplast, the mechanisms of lipid transport within and between chloroplast membranes remain elusive. This dissertation provides insight into this fundamental knowledge gap of plant biology by expounding on known lipid transport and remodeling pathways that occur at the chloroplast as well as contributing experimental evidence for the role of intra-organellar membrane contact sites as mechanisms of lipid transfer to the innermost thylakoid membrane. The proteome of the thylakoid-inner envelope interface is uncovered here, serving as a platform for intra-organellar membrane contact site discovery. Furthermore, lipid movement functionality of the chloroplast-localized Tvp38 homology protein TVPFP is established, thus implicating its probable association with lipid transfer to the thylakoid. In all, these findings enhance our current understanding of chloroplast lipid transport, particularly pertaining to the thylakoid.

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