Nfs1 cysteine desulfurase protein complexes and phosphorylation sites as assessed by mass spectrometry

Agostinho G. Rocha; Simon A.B. Knight; Alok Pandey; Heeyong Yoon; Jayashree Pain; Debkumar Pain; Andrew Dancis

doi:10.1016/j.dib.2017.09.068

Nfs1 cysteine desulfurase protein complexes and phosphorylation sites as assessed by mass spectrometry

Agostinho G. Rocha, Simon A.B. Knight, Alok Pandey, Heeyong Yoon, Jayashree Pain, Debkumar Pain, Andrew Dancis

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Abstract

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].

Original language	English (US)
Pages (from-to)	775-799
Number of pages	25
Journal	Data in Brief
Volume	15
DOIs	https://doi.org/10.1016/j.dib.2017.09.068
State	Published - Dec 2017

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@article{c588753d34834e2cb101ef34af31f2d9,

title = "Nfs1 cysteine desulfurase protein complexes and phosphorylation sites as assessed by mass spectrometry",

abstract = "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].",

author = "Rocha, {Agostinho G.} and Knight, {Simon A.B.} and Alok Pandey and Heeyong Yoon and Jayashree Pain and Debkumar Pain and Andrew Dancis",

note = "Funding Information: The authors thank Dr. Hsin-Yao Tang at the Wistar Institute Proteomics Facility for his assistance on the analysis of proteomics data. This work was supported by National Institutes of Health Grant DK053953 (to A.D.), and R01GM107542 (to D.P. and A.D.). Transparency document Publisher Copyright: {\textcopyright} 2017 The Authors",

year = "2017",

month = dec,

doi = "10.1016/j.dib.2017.09.068",

language = "English (US)",

volume = "15",

pages = "775--799",

journal = "Data in Brief",

issn = "2352-3409",

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TY - JOUR

T1 - Nfs1 cysteine desulfurase protein complexes and phosphorylation sites as assessed by mass spectrometry

AU - Rocha, Agostinho G.

AU - Knight, Simon A.B.

AU - Pandey, Alok

AU - Yoon, Heeyong

AU - Pain, Jayashree

AU - Pain, Debkumar

AU - Dancis, Andrew

N1 - Funding Information: The authors thank Dr. Hsin-Yao Tang at the Wistar Institute Proteomics Facility for his assistance on the analysis of proteomics data. This work was supported by National Institutes of Health Grant DK053953 (to A.D.), and R01GM107542 (to D.P. and A.D.). Transparency document Publisher Copyright: © 2017 The Authors

PY - 2017/12

Y1 - 2017/12

N2 - 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].

AB - 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].

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U2 - 10.1016/j.dib.2017.09.068

DO - 10.1016/j.dib.2017.09.068

M3 - Article

AN - SCOPUS:85032921066

SN - 2352-3409

VL - 15

SP - 775

EP - 799

JO - Data in Brief

JF - Data in Brief

ER -

Nfs1 cysteine desulfurase protein complexes and phosphorylation sites as assessed by mass spectrometry

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