Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation

Autor: Willy V Bienvenut, Annika Brünje, Jean‐Baptiste Boyer, Jens S Mühlenbeck, Gautier Bernal, Ines Lassowskat, Cyril Dian, Eric Linster, Trinh V Dinh, Minna M Koskela, Vincent Jung, Julian Seidel, Laura K Schyrba, Aiste Ivanauskaite, Jürgen Eirich, Rüdiger Hell, Dirk Schwarzer, Paula Mulo, Markus Wirtz, Thierry Meinnel, Carmela Giglione, Iris Finkemeier

Publikováno v: Molecular Systems Biology, Vol 16, Iss 7, Pp 1-23 (2020)

Abstract Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation (NTA) and ε‐lysine acetylation (KA) are known to be catalyzed by distinct families o

Externí odkaz: https://doaj.org/article/d26b41bab41445bf8117bc4fba9d0b24

An Acyl-CoA N-Acyltransferase Regulates Meristem Phase Change and Plant Architecture in Barley

Autor: Agatha Walla, Gwendolyn K. Kirschner, Iris Finkemeier, Rüdiger Simon, Ganggang Guo, G. Wilma van Esse, Maria von Korff, Annika Brünje

Publikováno v: Plant Physiology, 183(3), 1088-1109
Plant Physiology 183 (2020) 3
Plant Physiology

The modification of shoot architecture and increased investment into reproductive structures is key for crop improvement and is achieved through coordinated changes in the development and determinacy of different shoot meristems. A fundamental questi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98ae1e36323f41b6a905d6853c402153
https://doi.org/10.1104/pp.20.00087

NAA50 is an enzymatically active Nα-acetyltransferase that is crucial for development and regulation of stress responses

Autor: Eric Linster, Willy V. Bienvenut, Markus Wirtz, Carmela Giglione, Thierry Meinnel, Jürgen Eirich, Jonas Weidenhausen, Iris Finkemeier, Ruediger Hell, Jean-Baptiste Boyer, Iwona Stephan, Irmgard Sinning, Laura Armbruster, Annika Brünje

Publikováno v: Plant Physiology
Plant Physiology, 2020, 182 (2), pp.792-806. ⟨10.1104/pp.20.00222⟩
Plant Physiology, American Society of Plant Biologists, 2020, 182 (2), pp.792-806. ⟨10.1104/pp.20.00222⟩
Plant Physiology, American Society of Plant Biologists, 2020, 183 (4), pp.1502-1516. ⟨10.1104/pp.20.00222⟩
Plant Physiology, 2020, 183 (4), pp.1502-1516. ⟨10.1104/pp.20.00222⟩

International audience; N a-terminal acetylation (NTA) is a prevalent protein modification in eukaryotes. In plants, the biological function of NTA remains enigmatic. The dominant N-acetyltransferase (Nat) in Arabidopsis (Arabidopsis thaliana) is Nat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::663735bded8b6880418d43a13bcd856e
http://hdl.handle.net/20.500.12278/113192

The Arabidopsis N$^\alpha$ -acetyltransferase NAA60 locates to the plasma membrane and is vital for the high salt stress response

Autor: Dirk Schwarzer, Trinh V. Dinh, Iris Finkemeier, Felix Alexander Weyer, Ruediger Hell, Dominik Layer, Pavlina Miklankova, Irmgard Sinning, Willy V. Bienvenut, Carmela Giglione, Marion Hoffrichter, Eric Linster, Jürgen Kopp, Annika Brünje, Markus Wirtz, Karine Lapouge, Julia Sindlinger, Thierry Meinnel, Wiebke Leemhuis

Publikováno v: New Phytologist
New Phytologist, Wiley, 2020, ⟨10.1111/nph.16747⟩
New Phytologist, 2020, ⟨10.1111/nph.16747⟩
'New Phytologist ', vol: 228, pages: 554-569 (2020)
New Phytologist, Wiley, 2020, 228 (2), pp.554-669. ⟨10.1111/nph.16747⟩
New Phytologist, 2020, 228 (2), pp.554-669. ⟨10.1111/nph.16747⟩

International audience; In humans and plants, N-terminal acetylation plays a central role in protein homeostasis, affects 80 % of proteins in the cytoplasm and is catalyzed by five ribosome-associated N-acetyltransferases (NatA-E). Humans also posses

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fb74ba67b8a66ad17243c3431a9fcfc
https://hal.archives-ouvertes.fr/hal-02877932

Hydride Binding to the Active Site of [FeFe]-Hydrogenase

Autor: Thomas Happe, Matthias Driess, Kajsa G.V. Sigfridsson, Shenglai Yao, Christian Limberg, Nils Leidel, Rafael Schiwon, Michael Haumann, Annika Brünje, Petko Chernev, Ramona Kositzki, Camilla Lambertz, Chung-Hung Hsieh

Publikováno v: Inorganic Chemistry. 53:12164-12177

[FeFe]-hydrogenase from green algae (HydA1) is the most efficient hydrogen (H2) producing enzyme in nature and of prime interest for (bio)technology. Its active site is a unique six-iron center (H-cluster) composed of a cubane cluster, [4Fe4S]H, cyst

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0428a652ec592818d75d62eb8e84dda
https://doi.org/10.1021/ic502047q