A Global Proteomic Approach Sheds New Light on Potential Iron-Sulfur Client Proteins of the Chloroplastic Maturation Factor NFU3
Iron-sulfur (Fe-S) proteins play critical functions in plants. Most Fe-S proteins are synthetized in the cytosol as apo-proteins and the subsequent Fe-S cluster incorporation relies on specific protein assembly machineries. They are notably formed by a scaffold complex, which serves for the de novo...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-10-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/21/21/8121 |
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| author | Nathalie Berger Florence Vignols Brigitte Touraine Maël Taupin-Broggini Valérie Rofidal Vincent Demolombe Véronique Santoni Nicolas Rouhier Frédéric Gaymard Christian Dubos |
| author_facet | Nathalie Berger Florence Vignols Brigitte Touraine Maël Taupin-Broggini Valérie Rofidal Vincent Demolombe Véronique Santoni Nicolas Rouhier Frédéric Gaymard Christian Dubos |
| author_sort | Nathalie Berger |
| collection | DOAJ |
| description | Iron-sulfur (Fe-S) proteins play critical functions in plants. Most Fe-S proteins are synthetized in the cytosol as apo-proteins and the subsequent Fe-S cluster incorporation relies on specific protein assembly machineries. They are notably formed by a scaffold complex, which serves for the de novo Fe-S cluster synthesis, and by transfer proteins that insure cluster delivery to apo-targets. However, scarce information is available about the maturation pathways of most plastidial Fe-S proteins and their specificities towards transfer proteins of the associated SUF machinery. To gain more insights into these steps, the expression and protein localization of the NFU1, NFU2, and NFU3 transfer proteins were analyzed in various <i>Arabidopsis thaliana</i> organs and tissues showing quite similar expression patterns. In addition, quantitative proteomic analysis of an <i>nfu3</i> loss-of-function mutant allowed to propose novel potential client proteins for NFU3 and to show that the protein accumulation profiles and thus metabolic adjustments differ substantially from those established in the <i>nfu2</i> mutant. By clarifying the respective roles of the three plastidial NFU paralogs, these data allow better delineating the maturation process of plastidial Fe-S proteins. |
| first_indexed | 2024-03-10T15:12:09Z |
| format | Article |
| id | doaj.art-970249123af24b3da4d5d6637b6727d3 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T15:12:09Z |
| publishDate | 2020-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-970249123af24b3da4d5d6637b6727d32023-11-20T19:15:59ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-10-012121812110.3390/ijms21218121A Global Proteomic Approach Sheds New Light on Potential Iron-Sulfur Client Proteins of the Chloroplastic Maturation Factor NFU3Nathalie Berger0Florence Vignols1Brigitte Touraine2Maël Taupin-Broggini3Valérie Rofidal4Vincent Demolombe5Véronique Santoni6Nicolas Rouhier7Frédéric Gaymard8Christian Dubos9BPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, FranceBPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, FranceBPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, FranceBPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, FranceBPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, FranceBPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, FranceBPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, FranceUniversité de Lorraine, INRAE, IAM, F-54000 Nancy, FranceBPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, FranceBPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, FranceIron-sulfur (Fe-S) proteins play critical functions in plants. Most Fe-S proteins are synthetized in the cytosol as apo-proteins and the subsequent Fe-S cluster incorporation relies on specific protein assembly machineries. They are notably formed by a scaffold complex, which serves for the de novo Fe-S cluster synthesis, and by transfer proteins that insure cluster delivery to apo-targets. However, scarce information is available about the maturation pathways of most plastidial Fe-S proteins and their specificities towards transfer proteins of the associated SUF machinery. To gain more insights into these steps, the expression and protein localization of the NFU1, NFU2, and NFU3 transfer proteins were analyzed in various <i>Arabidopsis thaliana</i> organs and tissues showing quite similar expression patterns. In addition, quantitative proteomic analysis of an <i>nfu3</i> loss-of-function mutant allowed to propose novel potential client proteins for NFU3 and to show that the protein accumulation profiles and thus metabolic adjustments differ substantially from those established in the <i>nfu2</i> mutant. By clarifying the respective roles of the three plastidial NFU paralogs, these data allow better delineating the maturation process of plastidial Fe-S proteins.https://www.mdpi.com/1422-0067/21/21/8121chloroplastquantitative proteomiciron-sulfur clusterArabidopsismaturation factorNFU1 |
| spellingShingle | Nathalie Berger Florence Vignols Brigitte Touraine Maël Taupin-Broggini Valérie Rofidal Vincent Demolombe Véronique Santoni Nicolas Rouhier Frédéric Gaymard Christian Dubos A Global Proteomic Approach Sheds New Light on Potential Iron-Sulfur Client Proteins of the Chloroplastic Maturation Factor NFU3 International Journal of Molecular Sciences chloroplast quantitative proteomic iron-sulfur cluster Arabidopsis maturation factor NFU1 |
| title | A Global Proteomic Approach Sheds New Light on Potential Iron-Sulfur Client Proteins of the Chloroplastic Maturation Factor NFU3 |
| title_full | A Global Proteomic Approach Sheds New Light on Potential Iron-Sulfur Client Proteins of the Chloroplastic Maturation Factor NFU3 |
| title_fullStr | A Global Proteomic Approach Sheds New Light on Potential Iron-Sulfur Client Proteins of the Chloroplastic Maturation Factor NFU3 |
| title_full_unstemmed | A Global Proteomic Approach Sheds New Light on Potential Iron-Sulfur Client Proteins of the Chloroplastic Maturation Factor NFU3 |
| title_short | A Global Proteomic Approach Sheds New Light on Potential Iron-Sulfur Client Proteins of the Chloroplastic Maturation Factor NFU3 |
| title_sort | global proteomic approach sheds new light on potential iron sulfur client proteins of the chloroplastic maturation factor nfu3 |
| topic | chloroplast quantitative proteomic iron-sulfur cluster Arabidopsis maturation factor NFU1 |
| url | https://www.mdpi.com/1422-0067/21/21/8121 |
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