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The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX
IscX (or YfhJ) is a protein of unknown function which takes part in the iron-sulfur cluster assembly machinery, a highly specialized and essential metabolic pathway. IscX binds to iron with low affinity and interacts with IscS, the desulfurase central to cluster assembly. Previous studies have sugge...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2018
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5801593/ https://www.ncbi.nlm.nih.gov/pubmed/29457004 http://dx.doi.org/10.3389/fmolb.2017.00097 |
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author | Adinolfi, Salvatore Puglisi, Rita Crack, Jason C. Iannuzzi, Clara Dal Piaz, Fabrizio Konarev, Petr V. Svergun, Dmitri I. Martin, Stephen Le Brun, Nick E. Pastore, Annalisa |
author_facet | Adinolfi, Salvatore Puglisi, Rita Crack, Jason C. Iannuzzi, Clara Dal Piaz, Fabrizio Konarev, Petr V. Svergun, Dmitri I. Martin, Stephen Le Brun, Nick E. Pastore, Annalisa |
author_sort | Adinolfi, Salvatore |
collection | PubMed |
description | IscX (or YfhJ) is a protein of unknown function which takes part in the iron-sulfur cluster assembly machinery, a highly specialized and essential metabolic pathway. IscX binds to iron with low affinity and interacts with IscS, the desulfurase central to cluster assembly. Previous studies have suggested a competition between IscX and CyaY, the bacterial ortholog of frataxin, for the same binding surface of IscS. This competition could suggest a link between the two proteins with a functional significance. Using a hybrid approach based on nuclear magnetic resonance, small angle scattering and biochemical methods, we show here that IscX is a modulator of the inhibitory properties of CyaY: by competing for the same site on IscS, the presence of IscX rescues the rates of enzymatic cluster formation which are inhibited by CyaY. The effect is stronger at low iron concentrations, whereas it becomes negligible at high iron concentrations. These results strongly suggest the mechanism of the dual regulation of iron sulfur cluster assembly under the control of iron as the effector. |
format | Online Article Text |
id | pubmed-5801593 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-58015932018-02-16 The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX Adinolfi, Salvatore Puglisi, Rita Crack, Jason C. Iannuzzi, Clara Dal Piaz, Fabrizio Konarev, Petr V. Svergun, Dmitri I. Martin, Stephen Le Brun, Nick E. Pastore, Annalisa Front Mol Biosci Molecular Biosciences IscX (or YfhJ) is a protein of unknown function which takes part in the iron-sulfur cluster assembly machinery, a highly specialized and essential metabolic pathway. IscX binds to iron with low affinity and interacts with IscS, the desulfurase central to cluster assembly. Previous studies have suggested a competition between IscX and CyaY, the bacterial ortholog of frataxin, for the same binding surface of IscS. This competition could suggest a link between the two proteins with a functional significance. Using a hybrid approach based on nuclear magnetic resonance, small angle scattering and biochemical methods, we show here that IscX is a modulator of the inhibitory properties of CyaY: by competing for the same site on IscS, the presence of IscX rescues the rates of enzymatic cluster formation which are inhibited by CyaY. The effect is stronger at low iron concentrations, whereas it becomes negligible at high iron concentrations. These results strongly suggest the mechanism of the dual regulation of iron sulfur cluster assembly under the control of iron as the effector. Frontiers Media S.A. 2018-02-02 /pmc/articles/PMC5801593/ /pubmed/29457004 http://dx.doi.org/10.3389/fmolb.2017.00097 Text en Copyright © 2018 Adinolfi, Puglisi, Crack, Iannuzzi, Dal Piaz, Konarev, Svergun, Martin, Le Brun and Pastore. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Molecular Biosciences Adinolfi, Salvatore Puglisi, Rita Crack, Jason C. Iannuzzi, Clara Dal Piaz, Fabrizio Konarev, Petr V. Svergun, Dmitri I. Martin, Stephen Le Brun, Nick E. Pastore, Annalisa The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX |
title | The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX |
title_full | The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX |
title_fullStr | The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX |
title_full_unstemmed | The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX |
title_short | The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX |
title_sort | molecular bases of the dual regulation of bacterial iron sulfur cluster biogenesis by cyay and iscx |
topic | Molecular Biosciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5801593/ https://www.ncbi.nlm.nih.gov/pubmed/29457004 http://dx.doi.org/10.3389/fmolb.2017.00097 |
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