The Plastidial Protein Acetyltransferase GNAT1 Forms a Complex With GNAT2, yet Their Interaction Is Dispensable for State Transitions
In BriefProtein acetylation is a common cotranslational and posttranslational modification in chloroplasts.Here, we characterize GNAT1, an acetyltransferase that adds acetyl groups to N-termini and lysine side chains.GNAT1 is closely related to GNAT2, which regulates state transitions of the photosynthetic antenna proteins.Our findings show shared Nterminal substrate sites between GNAT1 and GNAT2 in vivo.Both enzymes form a complex, but this interaction is not essential for state transitions. Highlights GNAT1 is a plastidial acetyltransferase with dual activity in Arabidopsis. The N-terminal substrates of GNAT1 form a subset of the substrate set of GNAT2. Predicted structure models of GNAT1 and GNAT2 show a high architectural similarity. Absence of GNAT1 neither impacts state transitions nor acclimation to high light. Stable interactions were observed between GNAT1 & GNAT2 and GNAT2 & GNAT3.
Authors
- Annika Brünje (ORCID: https://orcid.org/0000-0002-8979-4606)
- Jürgen Eirich
- Wataru Sakamoto (ORCID: https://orcid.org/0000-0001-9747-5042)
- Iris Finkemeier (ORCID: https://orcid.org/0000-0002-8972-4026)
- Dirk Schwarzer (ORCID: https://orcid.org/0000-0002-7477-3319)
- Shin‐Ichiro Ozawa (ORCID: https://orcid.org/0000-0001-7698-5350)
- Ulla Neumann (ORCID: https://orcid.org/0000-0001-9200-4209)
- Aiste Ivanauskaite (ORCID: https://orcid.org/0000-0002-1149-5243)
- Paula Mulo (ORCID: https://orcid.org/0000-0002-8728-3204)
- J. Boyer (ORCID: https://orcid.org/0000-0001-5265-3917)
- Minna M. Konert (ORCID: https://orcid.org/0000-0002-6363-1470)
- Thierry Meinnel (ORCID: https://orcid.org/0000-0001-5642-8637)
- Carmela Giglione (ORCID: https://orcid.org/0000-0002-7475-1558)
- Julian Seidel (ORCID: https://orcid.org/0000-0002-0435-3845)
- Magdalena Füßl
- Paulina Heinkow (ORCID: https://orcid.org/0000-0002-0038-402X)
Institutions
- Centre National de la Recherche Scientifique (FR)
- Okayama University of Science (JP)
- University of Turku (FI)
- Okayama University (JP)
- Forschungszentrum Jülich (DE)
- University of Münster (DE)
- Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR)
- Université Paris-Saclay (FR)
- Gesellschaft für Klinische Forschung (DE)
- Institute of Plant Biology and Biotechnology (KZ)
- Institut de Biologie Intégrative de la Cellule (FR)
- Institut de Biologie Physico-Chimique (FR)
- CEA Paris-Saclay (FR)
- Helmholtz-Institute Münster (DE)
- Max Planck Institute for Plant Breeding Research (DE)
- Biologie du Chloroplaste et Perception de la Lumière chez les Microalgues (FR)
- University of Tübingen (DE)
Publication Details
- Journal
- Molecular & Cellular Proteomics
- Published
- 2024-09-28
- DOI
- https://doi.org/10.1016/j.mcpro.2024.100850
- Citations
- 6
- Primary Topic
- Enzyme Structure and Function
- Type
- article
- Field-Weighted Citation Impact
- 0.70
Funders
- Infrastructures en Biologie Santé et Agronomie
- European Cooperation in Science and Technology
- Deutscher Akademischer Austauschdienst
- Deutsche Forschungsgemeinschaft
- Agence Nationale de la Recherche
- Centre National de la Recherche Scientifique
- Okayama University
- Japan Society for the Promotion of Science