The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis
Mitochondrial fatty acid synthesis (FASII) and iron sulfur cluster (FeS) biogenesis are both vital biosynthetic processes within mitochondria. In this study, we demonstrate that the mitochondrial acyl carrier protein (ACP), which has a well-known role in FASII, plays an unexpected and evolutionarily...
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2016-08-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/17828 |
| _version_ | 1811236848324837376 |
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| author | Jonathan G Van Vranken Mi-Young Jeong Peng Wei Yu-Chan Chen Steven P Gygi Dennis R Winge Jared Rutter |
| author_facet | Jonathan G Van Vranken Mi-Young Jeong Peng Wei Yu-Chan Chen Steven P Gygi Dennis R Winge Jared Rutter |
| author_sort | Jonathan G Van Vranken |
| collection | DOAJ |
| description | Mitochondrial fatty acid synthesis (FASII) and iron sulfur cluster (FeS) biogenesis are both vital biosynthetic processes within mitochondria. In this study, we demonstrate that the mitochondrial acyl carrier protein (ACP), which has a well-known role in FASII, plays an unexpected and evolutionarily conserved role in FeS biogenesis. ACP is a stable and essential subunit of the eukaryotic FeS biogenesis complex. In the absence of ACP, the complex is destabilized resulting in a profound depletion of FeS throughout the cell. This role of ACP depends upon its covalently bound 4’-phosphopantetheine (4-PP)-conjugated acyl chain to support maximal cysteine desulfurase activity. Thus, it is likely that ACP is not simply an obligate subunit but also exploits the 4-PP-conjugated acyl chain to coordinate mitochondrial fatty acid and FeS biogenesis. |
| first_indexed | 2024-04-12T12:16:13Z |
| format | Article |
| id | doaj.art-ef650ab972b34957aca76d60cf881293 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T12:16:13Z |
| publishDate | 2016-08-01 |
| publisher | eLife Sciences Publications Ltd |
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| series | eLife |
| spelling | doaj.art-ef650ab972b34957aca76d60cf8812932022-12-22T03:33:26ZengeLife Sciences Publications LtdeLife2050-084X2016-08-01510.7554/eLife.17828The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesisJonathan G Van Vranken0https://orcid.org/0000-0002-8931-852XMi-Young Jeong1Peng Wei2Yu-Chan Chen3Steven P Gygi4Dennis R Winge5https://orcid.org/0000-0003-1160-1189Jared Rutter6https://orcid.org/0000-0002-2710-9765Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United StatesDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States; Department of Medicine, University of Utah School of Medicine, Salt Lake City, United StatesDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United StatesDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United StatesDepartment of Cell Biology, Harvard University School of Medicine, Boston, United StatesDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States; Department of Medicine, University of Utah School of Medicine, Salt Lake City, United StatesDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States; Howard Hughes Medical Institute, University of Utah School of Medicine, Salt Lake City, United StatesMitochondrial fatty acid synthesis (FASII) and iron sulfur cluster (FeS) biogenesis are both vital biosynthetic processes within mitochondria. In this study, we demonstrate that the mitochondrial acyl carrier protein (ACP), which has a well-known role in FASII, plays an unexpected and evolutionarily conserved role in FeS biogenesis. ACP is a stable and essential subunit of the eukaryotic FeS biogenesis complex. In the absence of ACP, the complex is destabilized resulting in a profound depletion of FeS throughout the cell. This role of ACP depends upon its covalently bound 4’-phosphopantetheine (4-PP)-conjugated acyl chain to support maximal cysteine desulfurase activity. Thus, it is likely that ACP is not simply an obligate subunit but also exploits the 4-PP-conjugated acyl chain to coordinate mitochondrial fatty acid and FeS biogenesis.https://elifesciences.org/articles/17828acyl carrier proteinmitochondrial fatty acid synthesisiron sulfur cluster biogenesis |
| spellingShingle | Jonathan G Van Vranken Mi-Young Jeong Peng Wei Yu-Chan Chen Steven P Gygi Dennis R Winge Jared Rutter The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis eLife acyl carrier protein mitochondrial fatty acid synthesis iron sulfur cluster biogenesis |
| title | The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis |
| title_full | The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis |
| title_fullStr | The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis |
| title_full_unstemmed | The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis |
| title_short | The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis |
| title_sort | mitochondrial acyl carrier protein acp coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis |
| topic | acyl carrier protein mitochondrial fatty acid synthesis iron sulfur cluster biogenesis |
| url | https://elifesciences.org/articles/17828 |
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