Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae

nifU of nitrogen-fixing bacteria is involved in the synthesis of the Fe–S cluster of nitrogenase. In a synthetic lethal screen with the mitochondrial heat shock protein (HSP)70, SSQ1, we identified a gene of Saccharomyces cerevisiae, NFU1, which encodes a protein with sequence identity to the C-term...

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Main Authors: Schilke, Brenda, Voisine, Cindy, Beinert, Helmut, Craig, Elizabeth
Formato: Artigo
Idioma:en
Publicado em: The National Academy of Sciences 1999
Assuntos:
Biological Sciences
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC17867/
https://ncbi.nlm.nih.gov/pubmed/10468587
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spelling pubmed-178672001-03-08 Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae Schilke, Brenda Voisine, Cindy Beinert, Helmut Craig, Elizabeth Proc Natl Acad Sci U S A Biological Sciences nifU of nitrogen-fixing bacteria is involved in the synthesis of the Fe–S cluster of nitrogenase. In a synthetic lethal screen with the mitochondrial heat shock protein (HSP)70, SSQ1, we identified a gene of Saccharomyces cerevisiae, NFU1, which encodes a protein with sequence identity to the C-terminal domain of NifU. Two other yeast genes were found to encode proteins related to the N-terminal domain of bacterial NifU. They have been designated ISU1 and ISU2. Isu1, Isu2, and Nfu1 are located in the mitochondrial matrix. ISU genes of yeast carry out an essential function, because a Δisu1Δisu2 strain is inviable. Growth of Δnfu1Δ isu1 cells is significantly compromised, allowing assessment of the physiological roles of Nfu and Isu proteins. Mitochondria from Δnfu1Δisu1 cells have decreased activity of several respiratory enzymes that contain Fe–S clusters. As a result, Δnfu1Δisu1 cells grow poorly on carbon sources requiring respiration. Δnfu1Δisu1 cells also accumulate abnormally high levels of iron in their mitochondria, similar to Δssq1 cells, indicating a role for these proteins in iron metabolism. We suggest that NFU1 and ISU1 gene products play a role in iron homeostasis, perhaps in assembly, insertion, and/or repair of mitochondrial Fe–S clusters. The conservation of these protein domains in many organisms suggests that this role has been conserved throughout evolution. The National Academy of Sciences 1999-08-31 /pmc/articles/PMC17867/ /pubmed/10468587 Text en Copyright © 1999, The National Academy of Sciences
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Biological Sciences
spellingShingle Biological Sciences
Schilke, Brenda
Voisine, Cindy
Beinert, Helmut
Craig, Elizabeth
Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
description nifU of nitrogen-fixing bacteria is involved in the synthesis of the Fe–S cluster of nitrogenase. In a synthetic lethal screen with the mitochondrial heat shock protein (HSP)70, SSQ1, we identified a gene of Saccharomyces cerevisiae, NFU1, which encodes a protein with sequence identity to the C-terminal domain of NifU. Two other yeast genes were found to encode proteins related to the N-terminal domain of bacterial NifU. They have been designated ISU1 and ISU2. Isu1, Isu2, and Nfu1 are located in the mitochondrial matrix. ISU genes of yeast carry out an essential function, because a Δisu1Δisu2 strain is inviable. Growth of Δnfu1Δ isu1 cells is significantly compromised, allowing assessment of the physiological roles of Nfu and Isu proteins. Mitochondria from Δnfu1Δisu1 cells have decreased activity of several respiratory enzymes that contain Fe–S clusters. As a result, Δnfu1Δisu1 cells grow poorly on carbon sources requiring respiration. Δnfu1Δisu1 cells also accumulate abnormally high levels of iron in their mitochondria, similar to Δssq1 cells, indicating a role for these proteins in iron metabolism. We suggest that NFU1 and ISU1 gene products play a role in iron homeostasis, perhaps in assembly, insertion, and/or repair of mitochondrial Fe–S clusters. The conservation of these protein domains in many organisms suggests that this role has been conserved throughout evolution.
author Schilke, Brenda
Voisine, Cindy
Beinert, Helmut
Craig, Elizabeth
author_facet Schilke, Brenda
Voisine, Cindy
Beinert, Helmut
Craig, Elizabeth
author_sort Schilke, Brenda
title Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
title_short Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
title_full Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
title_fullStr Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
title_full_unstemmed Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
title_sort evidence for a conserved system for iron metabolism in the mitochondria of saccharomyces cerevisiae
publisher The National Academy of Sciences
publisher_facet The National Academy of Sciences
publishDate 1999
url https://ncbi.nlm.nih.gov/pmc/articles/PMC17867/
https://ncbi.nlm.nih.gov/pubmed/10468587
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