Abstract

Iron-containing proteins, including iron-sulfur (Fe-S) proteins, are essential for numerous electron transfer and metabolic reactions. They are present in most subcellular compartments. In plastids, in addition to sustaining the linear and cyclic photosynthetic electron transfer chains, Fe-S proteins participate in carbon, nitrogen, and sulfur assimilation, tetrapyrrole and isoprenoid metabolism, and lipoic acid and thiamine synthesis. The synthesis of Fe-S clusters, their trafficking, and their insertion into chloroplastic proteins necessitate the so-called sulfur mobilization (SUF) protein machinery. In the first part, we describe the molecular mechanisms that allow Fe-S cluster synthesis and insertion into acceptor proteins by the SUF machinery and analyze the occurrence of the SUF components in microalgae, focusing in particular on the green alga Chlamydomonas reinhardtii. In the second part, we describe chloroplastic Fe-S protein-dependent pathways that are specific to Chlamydomonas or for which Chlamydomonas presents specificities compared to terrestrial plants, putting notable emphasis on the contribution of Fe-S proteins to chlorophyll synthesis in the dark and to the fermentative metabolism. The occurrence and evolutionary conservation of these enzymes and pathways have been analyzed in all supergroups of microalgae performing oxygenic photosynthesis.

Highlights

  • Iron (Fe) is a highly abundant metal on earth, and was present at the origin of life in ferrous form (Fe2+ ) associated with sulfur in pyrite (FeS2 ), as well as contributing to electron transfer reactions

  • We focused on the chloroplastic Fe-S protein-dependent pathways that are specific to Chlamydomonas, or for which Chlamydomonas presents specificities compared to terrestrial plants

  • It is worth noting that Chlamydomonas and other close Chlorophyceae (Volvox carteri and Gonium pectorale) possess 12 genes coding for chloroplastic FDXs [56,57], which far surpasses the content of FDX genes in land plants, with six genes being present, for instance, in Arabidopsis [5]

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Summary

Introduction

Iron (Fe) is a highly abundant metal on earth, and was present at the origin of life in ferrous form (Fe2+ ) associated with sulfur in pyrite (FeS2 ), as well as contributing to electron transfer reactions. More complex and atypical Fe-S clusters are observed in nature, mainly in proteins (e.g., nitrogenases, hydrogenases (HYDs), hybrid cluster proteins (HCPs)) present in prokaryotes and in some primitive eukaryotes including microalgae [2]. All these diverse Fe-S cluster forms confer to the associated proteins a wide range of functions, such as electron, sulfur or iron atom donors, intracellular oxygen or. As for mitochondria [4], the chloroplast has a very high demand in Fe-S cofactors, notably in the photosynthetic electron transport chain [5] They are present in complexes involved in the linear electron transfer chain, including one (2Fe-2S) cluster in the Rieske subunit of the cytochrome b6 f, three (4Fe-4S) clusters in photosystem I (PSI) subunits, and one (2Fe-2S). We focused on the chloroplastic Fe-S protein-dependent pathways that are specific to Chlamydomonas, or for which Chlamydomonas presents specificities compared to terrestrial plants

Lessons from Escherichia coli and Arabidopsis thaliana
Working of Both the SUF
CDs usually require
D scaffold
Occurrence of the SUF Components in Microalgae
Fe-S Protein-Dependent Metabolic Processes in Algal Chloroplasts
Synthesis of Isoprenoids
Dark-Operative Protochlorophyllide a Oxidoreductase
Type I NADH Dehydrogenase in Microalgae
Photosystem II Protein 33
Chloroplast Sensor Kinase
Contribution of Fe-S Enzymes to the Fermentative Metabolism
Pyruvate-Formate Lyase Activating Enzyme
Pyruvate-Ferredoxin Oxidoreductase
Hydrogenases and Their Maturation Factors
Hybrid Cluster Protein
Sulfite Reductase
Fermentative Pathways in Other Microalgae
Findings
Conclusions
Full Text
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