Plasticity in the proteome of Emiliania huxleyi CCMP 1516 to extremes of light is highly targeted

© 2013 The Authors. New Phytologist © 2013 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 200(2013), 1 vom: 26. Okt., Seite 61-73
1. Verfasser: McKew, Boyd A (VerfasserIn)
Weitere Verfasser: Lefebvre, Stephane C, Achterberg, Eric P, Metodieva, Gergana, Raines, Christine A, Metodiev, Metodi V, Geider, Richard J
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Emiliania huxleyi LI818 high light light acclimation light harvesting low light shotgun proteomics Chlorophyll Binding Proteins mehr... Photosynthetic Reaction Center Complex Proteins Photosystem I Protein Complex Photosystem II Protein Complex Plant Proteins Proteome Xanthophylls fucoxanthin 06O0TC0VSM Chlorophyll 1406-65-1
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520 |a Optimality principles are often applied in theoretical studies of microalgal ecophysiology to predict changes in allocation of resources to different metabolic pathways, and optimal acclimation is likely to involve changes in the proteome, which typically accounts for > 50% of cellular nitrogen (N). We tested the hypothesis that acclimation of the microalga Emiliania huxleyi CCMP 1516 to suboptimal vs supraoptimal light involves large changes in the proteome as cells rebalance the capacities to absorb light, fix CO2 , perform biosynthesis and resist photooxidative stress. Emiliania huxleyi was grown in nutrient-replete continuous culture at 30 (LL) and 1000 μmol photons m(-2) s(-1) (HL), and changes in the proteome were assessed by LC-MS/MS shotgun proteomics. Changes were most evident in proteins involved in the light reactions of photosynthesis; the relative abundance of photosystem I (PSI) and PSII proteins was 70% greater in LL, light-harvesting fucoxanthin-chlorophyll proteins (Lhcfs) were up to 500% greater in LL and photoprotective LI818 proteins were 300% greater in HL. The marked changes in the abundances of Lhcfs and LI818s, together with the limited plasticity in the bulk of the E. huxleyi proteome, probably reflect evolutionary pressures to provide energy to maintain metabolic capabilities in stochastic light environments encountered by this species in nature 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Emiliania huxleyi 
650 4 |a LI818 
650 4 |a high light 
650 4 |a light acclimation 
650 4 |a light harvesting 
650 4 |a low light 
650 4 |a shotgun proteomics 
650 7 |a Chlorophyll Binding Proteins  |2 NLM 
650 7 |a Photosynthetic Reaction Center Complex Proteins  |2 NLM 
650 7 |a Photosystem I Protein Complex  |2 NLM 
650 7 |a Photosystem II Protein Complex  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Proteome  |2 NLM 
650 7 |a Xanthophylls  |2 NLM 
650 7 |a fucoxanthin  |2 NLM 
650 7 |a 06O0TC0VSM  |2 NLM 
650 7 |a Chlorophyll  |2 NLM 
650 7 |a 1406-65-1  |2 NLM 
700 1 |a Lefebvre, Stephane C  |e verfasserin  |4 aut 
700 1 |a Achterberg, Eric P  |e verfasserin  |4 aut 
700 1 |a Metodieva, Gergana  |e verfasserin  |4 aut 
700 1 |a Raines, Christine A  |e verfasserin  |4 aut 
700 1 |a Metodiev, Metodi V  |e verfasserin  |4 aut 
700 1 |a Geider, Richard J  |e verfasserin  |4 aut 
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