Protein assemblies in the Arabidopsis thaliana chloroplast compartment

authored by

Noah Ditz, Hans-Peter Braun, Holger Eubel

Abstract

INTRODUCTION: Equipped with a photosynthetic apparatus that uses the energy of solar radiation to fuel biosynthesis of organic compounds, chloroplasts are the metabolic factories of mature leaf cells. The first steps of energy conversion are catalyzed by a collection of protein complexes, which can dynamically interact with each other for optimizing metabolic efficiency under changing environmental conditions.

MATERIALS AND METHODS: For a deeper insight into the organization of protein assemblies and their roles in chloroplast adaption to changing environmental conditions, an improved complexome profiling protocol employing a MS-cleavable cross-linker is used to stabilize labile protein assemblies during the organelle isolation procedure.

RESULTS AND DISCUSSION: Changes in protein:protein interaction patterns of chloroplast proteins in response to four different light intensities are reported. High molecular mass assemblies of central chloroplast electron transfer chain components as well as the PSII repair machinery react to different light intensities. In addition, the chloroplast encoded RNA-polymerase complex was found to migrate at a molecular mass of ~8 MDa, well above its previously reported molecular mass. Complexome profiling data produced during the course of this study can be interrogated by interested readers via a web-based online resource (https://complexomemap.de/projectsinteraction-chloroplasts).

Organisation(s)

Institute of Plant Genetics

Type

Article

Journal

Frontiers in Plant Science

Volume

ISSN

1664-462X

Publication date

16.08.2024

Publication status

Published

Peer reviewed

Yes

ASJC Scopus subject areas

Plant Science

Electronic version(s)

https://doi.org/10.3389/fpls.2024.1380969 (Access: Open)