Heterotrifunctional Chemical Cross-Linking Mass Spectrometry Confirms Physical Interaction between Human Frataxin and ISU

The progressive neurodegenerative disease Friedreich’s ataxia is caused by a decreased level of expression of frataxin, a putative iron chaperone. Frataxin is thought to transiently interact with ISU, the scaffold protein onto which iron–sulfur clusters are assembled, to deliver ferrous iron. Photor...

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Bibliographic Details
Published in:Biochemistry (Easton) 2012-09, Vol.51 (35), p.6889-6891
Main Authors: Watson, Heather M, Gentry, Leslie E, Asuru, Awuri P, Wang, Yu, Marcus, Stevan, Busenlehner, Laura S
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Frataxin
Friedreich Ataxia - metabolism
Humans
Iron - metabolism
Iron-Binding Proteins - chemistry
Iron-Binding Proteins - metabolism
Iron-Sulfur Proteins - chemistry
Iron-Sulfur Proteins - metabolism
Models, Molecular
Molecular Sequence Data
Photochemical Processes
Protein Interaction Mapping
Sequence Alignment
Ultraviolet Rays
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Summary:The progressive neurodegenerative disease Friedreich’s ataxia is caused by a decreased level of expression of frataxin, a putative iron chaperone. Frataxin is thought to transiently interact with ISU, the scaffold protein onto which iron–sulfur clusters are assembled, to deliver ferrous iron. Photoreactive heterotrifunctional chemical cross-linking confirmed the interaction between frataxin and ISU in the presence of iron and validated that transient interactions can be covalently trapped with this method. Because frataxin may participate in transient interactions with other mitochondrial proteins, this cross-linking approach may reveal new protein partners and pathways in which it interacts and help deduce direct, downstream consequences of its deficiency.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi300779f