4.7 Article

Selenoprotein: Potential Player in Redox Regulation in Chlamydomonas reinhardtii

Journal

ANTIOXIDANTS
Volume 11, Issue 8, Pages -

Publisher

MDPI
DOI: 10.3390/antiox11081630

Keywords

selenoprotein; selenocysteine; antioxidants; algae; Chlamydomonas

Funding

  1. BioGreen21 Agri-Tech Innovation Program, Rural Development Administration, Republic of Korea [PJ01623501]
  2. Basic Science Research Program through the National Research Foundation of Korea (NRF) - Ministry of Education [2020R1A6A1A03044344, 2020R1F1A1074027, 2022R1I1A1A01064372]
  3. National Research Foundation of Korea [2022R1I1A1A01064372, 2020R1F1A1074027] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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Selenium is an essential microelement for many organisms, including Chlamydomonas reinhardtii. It is obtained from the amino acid selenocysteine and encoded by the UGA codon. Selenoproteins, proteins containing selenium, are present in animals and algae but not in fungi and higher plants. The human genome contains 25 selenoproteins, most of which play a role in antioxidant defense and redox regulation. In Chlamydomonas, 10 selenoprotein genes have been identified, and based on the conserved domains and catalytically active sites, it is suggested that Chlamydomonas selenoproteins may be involved in redox regulation and defense as antioxidants.
Selenium (Se) is an essential micro-element for many organisms, including Chlamydomonas reinhardtii, and is required in trace amounts. It is obtained from the 21st amino acid selenocysteine (Sec, U), genetically encoded by the UGA codon. Proteins containing Sec are known as selenoproteins. In eukaryotes, selenoproteins are present in animals and algae, whereas fungi and higher plants lack them. The human genome contains 25 selenoproteins, most of which are involved in antioxidant defense activity, redox regulation, and redox signaling. In algae, 42 selenoprotein families were identified using various bioinformatics approaches, out of which C. reinhardtii is known to have 10 selenoprotein genes. However, the role of selenoproteins in Chlamydomonas is yet to be reported. Chlamydomonas selenoproteins contain conserved domains such as CVNVGC and GCUG, in the case of thioredoxin reductase, and CXXU in other selenoproteins. Interestingly, Sec amino acid residue is present in a catalytically active domain in Chlamydomonas selenoproteins, similar to human selenoproteins. Based on catalytical active sites and conserved domains present in Chlamydomonas selenoproteins, we suggest that Chlamydomonas selenoproteins could have a role in redox regulation and defense by acting as antioxidants in various physiological conditions.

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