Details
| Original language | English |
|---|---|
| Article number | 1380969 |
| Pages (from-to) | 1380969 |
| Journal | Frontiers in Plant Science |
| Volume | 15 |
| Publication status | Published - 2024 |
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).
Keywords
- chloroplast transcription, cross-linking, high light, low light, photosynthesis, protein assembly, protein complexes, protein:protein interactions
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Plant Science
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In: Frontiers in Plant Science, Vol. 15, 1380969, 2024, p. 1380969.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Protein assemblies in the Arabidopsis thaliana chloroplast compartment.
AU - Ditz, Noah
AU - Braun, Hans-Peter
AU - Eubel, Holger
N1 - Copyright © 2024 Ditz, Braun and Eubel.
PY - 2024
Y1 - 2024
N2 - 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).
AB - 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).
KW - chloroplast transcription
KW - cross-linking
KW - high light
KW - low light
KW - photosynthesis
KW - protein assembly
KW - protein complexes
KW - protein:protein interactions
UR - http://www.scopus.com/inward/record.url?scp=85202748382&partnerID=8YFLogxK
U2 - 10.3389/fpls.2024.1380969
DO - 10.3389/fpls.2024.1380969
M3 - Article
C2 - 39220006
VL - 15
SP - 1380969
JO - Frontiers in Plant Science
JF - Frontiers in Plant Science
SN - 1664-462X
M1 - 1380969
ER -