A Light Switch Based on Protein S-Nitrosylation Fine-Tunes Photosynthetic Light Harvesting in Chlamydomonas

Berger H, De Mia M, Morisse S, Marchand CH, Lemaire SD, Wobbe L, Kruse O (2016)
PLANT PHYSIOLOGY 171(2): 821-832.

Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Autor
; ; ; ; ; ;
Abstract / Bemerkung
Photosynthetic eukaryotes are challenged by a fluctuating light supply, demanding for a modulated expression of nucleus-encoded light-harvesting proteins associated with photosystem II (LHCII) to adjust light-harvesting capacity to the prevailing light conditions. Here, we provide clear evidence for a regulatory circuit that controls cytosolic LHCII translation in response to light quantity changes. In the green unicellular alga Chlamydomonas reinhardtii, the cytosolic RNA-binding protein NAB1 represses translation of certain LHCII isoform mRNAs. Specific nitrosylation of Cys-226 decreases NAB1 activity and could be demonstrated in vitro and in vivo. The less active, nitrosylated form of NAB1 is found in cells acclimated to limiting light supply, which permits accumulation of light-harvesting proteins and efficient light capture. In contrast, elevated light supply causes its denitrosylation, thereby activating the repression of light-harvesting protein synthesis, which is needed to control excitation pressure at photosystem II. Denitrosylation of recombinant NAB1 is efficiently performed by the cytosolic thioredoxin system in vitro. To our knowledge, NAB1 is the first example of stimulus-induced denitrosylation in the context of photosynthetic acclimation. By identifying this novel redox cross-talk pathway between chloroplast and cytosol, we add a new key element required for drawing a precise blue print of the regulatory network of light harvesting.
Erscheinungsjahr
Zeitschriftentitel
PLANT PHYSIOLOGY
Band
171
Zeitschriftennummer
2
Seite
821-832
ISSN
eISSN
PUB-ID

Zitieren

Berger H, De Mia M, Morisse S, et al. A Light Switch Based on Protein S-Nitrosylation Fine-Tunes Photosynthetic Light Harvesting in Chlamydomonas. PLANT PHYSIOLOGY. 2016;171(2):821-832.
Berger, H., De Mia, M., Morisse, S., Marchand, C. H., Lemaire, S. D., Wobbe, L., & Kruse, O. (2016). A Light Switch Based on Protein S-Nitrosylation Fine-Tunes Photosynthetic Light Harvesting in Chlamydomonas. PLANT PHYSIOLOGY, 171(2), 821-832. doi:10.1104/pp.15.01878
Berger, H., De Mia, M., Morisse, S., Marchand, C. H., Lemaire, S. D., Wobbe, L., and Kruse, O. (2016). A Light Switch Based on Protein S-Nitrosylation Fine-Tunes Photosynthetic Light Harvesting in Chlamydomonas. PLANT PHYSIOLOGY 171, 821-832.
Berger, H., et al., 2016. A Light Switch Based on Protein S-Nitrosylation Fine-Tunes Photosynthetic Light Harvesting in Chlamydomonas. PLANT PHYSIOLOGY, 171(2), p 821-832.
H. Berger, et al., “A Light Switch Based on Protein S-Nitrosylation Fine-Tunes Photosynthetic Light Harvesting in Chlamydomonas”, PLANT PHYSIOLOGY, vol. 171, 2016, pp. 821-832.
Berger, H., De Mia, M., Morisse, S., Marchand, C.H., Lemaire, S.D., Wobbe, L., Kruse, O.: A Light Switch Based on Protein S-Nitrosylation Fine-Tunes Photosynthetic Light Harvesting in Chlamydomonas. PLANT PHYSIOLOGY. 171, 821-832 (2016).
Berger, Hanna, De Mia, Marcello, Morisse, Samuel, Marchand, Christophe H., Lemaire, Stephane D., Wobbe, Lutz, and Kruse, Olaf. “A Light Switch Based on Protein S-Nitrosylation Fine-Tunes Photosynthetic Light Harvesting in Chlamydomonas”. PLANT PHYSIOLOGY 171.2 (2016): 821-832.

3 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Protein S-Nitrosylation Regulates Xylem Vessel Cell Differentiation in Arabidopsis.
Kawabe H, Ohtani M, Kurata T, Sakamoto T, Demura T., Plant Cell Physiol 59(1), 2018
PMID: 29040725
The Deep Thioredoxome in Chlamydomonas reinhardtii: New Insights into Redox Regulation.
Pérez-Pérez ME, Mauriès A, Maes A, Tourasse NJ, Hamon M, Lemaire SD, Marchand CH., Mol Plant 10(8), 2017
PMID: 28739495

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 27208221
PubMed | Europe PMC

Suchen in

Google Scholar