Literature DB >> 33127356

Restoration of photosynthetic activity and supercomplexes from severe iron starvation in Chlamydomonas reinhardtii.

Elsinraju Devadasu1, Jayendra Pandey1, Kunal Dhokne1, Rajagopal Subramanyam2.   

Abstract

The eukaryotic alga Chlamydomonas (C.) reinhardtii is used as a model organism to study photosynthetic efficiency. We studied the organization and protein profile of thylakoid membranes under severe iron (Fe2+) deficiency condition and iron supplement for their restoration. Chlorophyll (Chl) a fluorescence fast OJIP transients were decreased in the severe Fe2+ deficient cells resulting in the reduction of the photochemical efficiency. The circular dichroism (CD) results from Fe2+ deficient thylakoid membranes show a significant change in pigment-pigment and pigment-protein excitonic interactions. The organization of super-complexes was also affected significantly. Furthermore, super-complexes of photosystem (PS) II and PSI, along with its dimers, were severely reduced. The complexes separated using sucrose gradient centrifugation shows that loss of super-complexes and excitonic pigment-pigment interactions were restored in the severely Fe2+ deficient cells upon Fe supplementation for three generations. Additionally, the immunoblots demonstrated that both PSII, PSI core, and their light-harvesting complex antenna proteins were differentially decreased. However, reduced core proteins were aggregated, which in turn proteins were unfold and destabilized the supercomplexes and its function. Interestingly, the aggregated proteins were insoluble after n-Dodecyl β-D-maltoside solubilization. Further, they were identified in the pellet form. When Fe2+ was added to the severely deficient cells, the photosynthetic activity, pigment-proteins complexes, and proteins were restored to the level of control after 3rd generation.
Copyright © 2020 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Chlamydomonas reinhardtti; Fe deficiency, recovery of photosystems; Pigment-protein complexes, protein aggregation; Super-complexes

Mesh:

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Year:  2020        PMID: 33127356     DOI: 10.1016/j.bbabio.2020.148331

Source DB:  PubMed          Journal:  Biochim Biophys Acta Bioenerg        ISSN: 0005-2728            Impact factor:   3.991


  3 in total

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