Phylogenetic analysis of the CDGSH iron-sulfur binding domain reveals its ancient origin

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dc.citation.articleNumber4840en_US
dc.citation.journalTitleScientific Reportsen_US
dc.citation.volumeNumber8en_US
dc.contributor.authorSengupta, Sohamen_US
dc.contributor.authorNechushtai, Rachelen_US
dc.contributor.authorJennings, Patricia A.en_US
dc.contributor.authorOnuchic, José N.en_US
dc.contributor.authorPadilla, Pamela A.en_US
dc.contributor.authorAzad, Rajeev K.en_US
dc.contributor.authorMittler, Ronen_US
dc.date.accessioned2018-07-16T21:54:26Zen_US
dc.date.available2018-07-16T21:54:26Zen_US
dc.date.issued2018en_US
dc.description.abstractThe iron-sulfur (2Fe-2S) binding motif CDGSH appears in many important plant and animal proteins that regulate iron and reactive oxygen metabolism. In human it is found in CISD1-3 proteins involved in diabetes, obesity, cancer, aging, cardiovascular disease and neurodegeneration. Despite the important biological role of the CDGSH domain, its origin, evolution and diversification, are largely unknown. Here, we report that: (1) the CDGSH domain appeared early in evolution, perhaps linked to the heavy use of iron-sulfur driven metabolism by early organisms; (2) a CISD3-like protein with two CDGSH domains on the same polypeptide appears to represent the ancient archetype of CDGSH proteins; (3) the origin of the human CISD3 protein is linked to the mitochondrial endosymbiotic event; (4) the CISD1/2 type proteins that contain only one CDGSH domain, but function as homodimers, originated after the divergence of bacteria and archaea/eukaryotes from their common ancestor; and (5) the human CISD1 and CISD2 proteins diverged about 650–720 million years ago, and CISD3 and CISD1/2 share their descent from an ancestral CISD about 1–1.1 billion years ago. Our findings reveal that the CDGSH domain is ancient in its origin and shed light on the complex evolutionary path of modern CDGSH proteins.en_US
dc.identifier.citationSengupta, Soham, Nechushtai, Rachel, Jennings, Patricia A., et al.. "Phylogenetic analysis of the CDGSH iron-sulfur binding domain reveals its ancient origin." <i>Scientific Reports,</i> 8, (2018) Springer Nature: https://doi.org/10.1038/s41598-018-23305-6.en_US
dc.identifier.doihttps://doi.org/10.1038/s41598-018-23305-6en_US
dc.identifier.urihttps://hdl.handle.net/1911/102443en_US
dc.language.isoengen_US
dc.publisherSpringer Natureen_US
dc.rightsThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder.en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en_US
dc.titlePhylogenetic analysis of the CDGSH iron-sulfur binding domain reveals its ancient originen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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