Nfs1 cysteine desulfurase protein complexes and phosphorylation sites as assessed by mass spectrometry
| Autor: | Andrew Dancis, Jayashree Pain, Heeyong Yoon, Alok Pandey, Debkumar Pain, Simon A.B. Knight, Agostinho G. Rocha |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Multidisciplinary biology Chemistry Kinase Cysteine desulfurase chemistry.chemical_element Mitochondrion lcsh:Computer applications to medicine. Medical informatics Mass spectrometry Sulfur Cofactor Yeast 03 medical and health sciences 030104 developmental biology Cell biology Biochemistry biology.protein lcsh:R858-859.7 Phosphorylation lcsh:Science (General) lcsh:Q1-390 |
| Zdroj: | Data in Brief, Vol 15, Iss, Pp 775-799 (2017) Data in Brief |
| ISSN: | 2352-3409 |
| Popis: | Fe-S clusters are cofactors that participate in diverse and essential biological processes. Mitochondria contain a complete machinery for Fe-S cluster assembly. Cysteine desulfurase (Nfs1) is required generation of a form of activated sulfur and is essential for the initial Fe-S cluster assembly step. Using mass-spectometry we identified proteins that were copurified with Nfs1 using a pull-down strategy, including a novel protein kinase. Furthermore, we were able to identify phosphorylation sites on the Nfs1 protein. These data and analyses support the research article “Cysteine desulfurase is regulated by phosphorylation of Nfs1 in yeast mitochondria” by Rocha et al. (in press) [1]. |
| Databáze: | OpenAIRE |
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