Journal: Nat Commun / Year: 2010 Title: Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Authors: Filippo Prischi / Petr V Konarev / Clara Iannuzzi / Chiara Pastore / Salvatore Adinolfi / Stephen R Martin / Dmitri I Svergun / Annalisa Pastore / Abstract: Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich's ataxia. Independent reports have linked frataxin ...Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich's ataxia. Independent reports have linked frataxin to iron-sulphur cluster assembly through interactions with the two central components of this machinery: desulphurase Nfs1/IscS and the scaffold protein Isu/IscU. In this study, we use a combination of biophysical methods to define the structural bases of the interaction of CyaY (the bacterial orthologue of frataxin) with the IscS/IscU complex. We show that CyaY binds IscS as a monomer in a pocket between the active site and the IscS dimer interface. Recognition does not require iron and occurs through electrostatic interactions of complementary charged residues. Mutations at the complex interface affect the rates of enzymatic cluster formation. CyaY binding strengthens the affinity of the IscS/IscU complex. Our data suggest a new paradigm for understanding the role of frataxin as a regulator of IscS functions.
Contact author
Petr Konarev (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)
Instrument name: DORIS III X33 / City: Hamburg / 国: Germany / Shape: 0.6 / Type of source: X-ray synchrotron / Wavelength: 0.15 Å / Dist. spec. to detc.: 2.7 mm
Detector
Name: Pilatus 1M-W / Pixsize x: 0.172 mm
Scan
Title: y / Measurement date: Nov 5, 2009 / Storage temperature: 15 °C / Cell temperature: 15 °C / Exposure time: 30 sec. / Number of frames: 4 / Unit: 1/nm /
Min
Max
Q
0.0775
6.237
Distance distribution function P(R)
Sofotware P(R): GNOM 4.5a / Number of points: 447 /
Min
Max
Q
0.2749
6.218
P(R) point
73
519
R
0
5.016
Result
D max: 5 / Type of curve: single_conc / Standard: bovin serum albumin Comments: Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich’s ataxia. Independent reports have ...Comments: Reduced levels of frataxin, an essential protein of as yet unknown function, are responsible for causing the neurodegenerative pathology Friedreich’s ataxia. Independent reports have linked frataxin to iron–sulphur cluster assembly through interactions with the two central components of this machinery: desulphurase Nfs1/IscS and the scaffold protein Isu/IscU. In this study, we use a combination of biophysical methods to define the structural bases of the
interaction of CyaY (the bacterial orthologue of frataxin) with the IscS/IscU complex. We show that CyaY binds IscS as a monomer in a pocket between the active site and the IscS dimer interface. Recognition does not require iron and occurs through electrostatic interactions of complementary charged residues. Mutations at the complex interface affect the rates of enzymatic cluster formation. CyaY binding strengthens the affinity of the IscS/IscU complex. Our data suggest a new paradigm for understanding the role of frataxin as a regulator of IscS functions.
Experimental
Standard
MW
11 kDa
11 kDa
P(R)
Guinier
Guinier error
Forward scattering, I0
14.8
14.8
-
Radius of gyration, Rg
1.53 nm
1.53 nm
0.004
+
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