期刊
SCIENTIFIC REPORTS
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/srep42571
关键词
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资金
- National Science Foundation [IOS-1557787, MCB-1613462]
- Israel Science Foundation [ISF 865/13]
- National Institutes of Health [DK54441]
- University of North Texas College of Arts and Sciences
- Cancer Prevention and Research Institute of Texas (CPRIT) [R1110]
- Center for Theoretical Biological Physics - NSF [PHY-1427654]
- [NSF-CHE 1614101]
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [1557787] Funding Source: National Science Foundation
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1614101, 1613462] Funding Source: National Science Foundation
- Direct For Mathematical & Physical Scien
- Division Of Physics [1427654] Funding Source: National Science Foundation
NEET proteins belong to a unique family of iron-sulfur proteins in which the 2Fe-2S cluster is coordinated by a CDGSH domain that is followed by the NEET motif. They are involved in the regulation of iron and reactive oxygen metabolism, and have been associated with the progression of diabetes, cancer, aging and neurodegenerative diseases. Despite their important biological functions, the evolution and diversification of eukaryotic NEET proteins are largely unknown. Here we used the three members of the human NEET protein family (CISD1, mitoNEET; CISD2, NAF-1 or Miner1; and CISD3, Miner2) as our guides to conduct a phylogenetic analysis of eukaryotic NEET proteins and their evolution. Our findings identified the slime mold Dictyostelium discoideum's CISD proteins as the closest to the ancient archetype of eukaryotic NEET proteins. We further identified CISD3 homologs in fungi that were previously reported not to contain any NEET proteins, and revealed that plants lack homolog(s) of CISD3. Furthermore, our study suggests that the mammalian NEET proteins, mitoNEET (CISD1) and NAF-1 (CISD2), emerged via gene duplication around the origin of vertebrates. Our findings provide new insights into the classification and expansion of the NEET protein family, as well as offer clues to the diverged functions of the human mitoNEET and NAF-1 proteins.
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