The identification of IsiA proteins binding chlorophyll d in the cyanobacterium Acaryochloris marina
Autor: | Zhong-Chun Zhang, Guo-Zheng Dai, Zheng-Ke Li, Yan-Chao Yin, Min Chen, Bao-Sheng Qiu, Lu-Dan Zhang |
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Rok vydání: | 2017 |
Předmět: |
Chlorophyll
0106 biological sciences 0301 basic medicine Photosystem II Iron Acaryochloris marina Chlorophyll d Plant Science Cyanobacteria Photosynthesis Thylakoids 01 natural sciences Biochemistry 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Doubling time Photosystem biology Temperature Plant physiology Cell Biology General Medicine biology.organism_classification Fluorescence Spectrometry Fluorescence 030104 developmental biology chemistry Multiprotein Complexes Chlorophyll Binding Proteins Protein Binding 010606 plant biology & botany |
Zdroj: | Photosynthesis Research. 135:165-175 |
ISSN: | 1573-5079 0166-8595 |
DOI: | 10.1007/s11120-017-0379-6 |
Popis: | The bioavailable iron in many aquatic ecosystems is extremely low, and limits the growth and photosynthetic activity of phytoplankton. In response to iron limitation, a group of chlorophyll-binding proteins known as iron stress-induced proteins are induced and serve as accessory light-harvesting components for photosystems under iron limitation. In the present study, we investigated physiological features of Acaryochloris marina in response to iron-deficient conditions. The growth doubling time under iron-deficient conditions was prolonged to ~3.4 days compared with 1.9 days under normal culture conditions, accompanied with dramatically decreased chlorophyll content. The isolation of chlorophyll-binding protein complexes using sucrose density gradient centrifugation shows six main green bands and three main fluorescence components of 712, 728, and 748 nm from the iron-deficient culture. The fluorescence components of 712 and 728 nm co-exist in the samples collected from iron-deficient and iron-replete cultures and are attributed to Chl d-binding accessory chlorophyll-binding antenna proteins and also from photosystem II. A new chlorophyll-binding protein complex with its main fluorescence peak at 748 nm was observed and enriched in the heaviest fraction from the samples collected from the iron-deficient culture only. Combining western blotting analysis using antibodies of CP47 (PSII), PsaC (PSI) and IsiA and proteomic analysis on an excised protein band at ~37 kDa, the heaviest fraction (-F6) isolated from iron-deficient culture contained Chl d-bound PSI-IsiA supercomplexes. The PSII-antenna supercomplexes isolated from iron-replete conditions showed two fluorescence peaks of 712 and 728 nm, which can be assigned as 6-transmembrane helix chlorophyll-binding antenna and photosystem II fluorescence, respectively, which is supported by protein analysis of the fractions (F5 and F6). |
Databáze: | OpenAIRE |
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