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A New Tessera into the Interactome of the isc Operon: A Novel Interaction between HscB and IscS
Iron sulfur clusters are essential universal prosthetic groups which can be formed inorganically but, in biology, are bound to proteins and produced enzymatically. Most of the components of the machine that produces the clusters are conserved throughout evolution. In bacteria, they are encoded in th...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5037179/ https://www.ncbi.nlm.nih.gov/pubmed/27730125 http://dx.doi.org/10.3389/fmolb.2016.00048 |
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author | Puglisi, Rita Yan, Robert Adinolfi, Salvatore Pastore, Annalisa |
author_facet | Puglisi, Rita Yan, Robert Adinolfi, Salvatore Pastore, Annalisa |
author_sort | Puglisi, Rita |
collection | PubMed |
description | Iron sulfur clusters are essential universal prosthetic groups which can be formed inorganically but, in biology, are bound to proteins and produced enzymatically. Most of the components of the machine that produces the clusters are conserved throughout evolution. In bacteria, they are encoded in the isc operon. Previous reports provide information on the role of specific components but a clear picture of how the whole machine works is still missing. We have carried out a study of the effects of the co-chaperone HscB from the model system E. coli. We document a previously undetected weak interaction between the chaperone HscB and the desulfurase IscS, one of the two main players of the machine. The binding site involves a region of HscB in the longer stem of the approximately L-shaped molecule, whereas the interacting surface of IscS overlaps with the surface previously involved in binding other proteins, such as ferredoxin and frataxin. Our findings provide an entirely new perspective to our comprehension of the role of HscB and propose this protein as a component of the IscS complex. |
format | Online Article Text |
id | pubmed-5037179 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-50371792016-10-11 A New Tessera into the Interactome of the isc Operon: A Novel Interaction between HscB and IscS Puglisi, Rita Yan, Robert Adinolfi, Salvatore Pastore, Annalisa Front Mol Biosci Molecular Biosciences Iron sulfur clusters are essential universal prosthetic groups which can be formed inorganically but, in biology, are bound to proteins and produced enzymatically. Most of the components of the machine that produces the clusters are conserved throughout evolution. In bacteria, they are encoded in the isc operon. Previous reports provide information on the role of specific components but a clear picture of how the whole machine works is still missing. We have carried out a study of the effects of the co-chaperone HscB from the model system E. coli. We document a previously undetected weak interaction between the chaperone HscB and the desulfurase IscS, one of the two main players of the machine. The binding site involves a region of HscB in the longer stem of the approximately L-shaped molecule, whereas the interacting surface of IscS overlaps with the surface previously involved in binding other proteins, such as ferredoxin and frataxin. Our findings provide an entirely new perspective to our comprehension of the role of HscB and propose this protein as a component of the IscS complex. Frontiers Media S.A. 2016-09-27 /pmc/articles/PMC5037179/ /pubmed/27730125 http://dx.doi.org/10.3389/fmolb.2016.00048 Text en Copyright © 2016 Puglisi, Yan, Adinolfi 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) or licensor 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 Puglisi, Rita Yan, Robert Adinolfi, Salvatore Pastore, Annalisa A New Tessera into the Interactome of the isc Operon: A Novel Interaction between HscB and IscS |
title | A New Tessera into the Interactome of the isc Operon: A Novel Interaction between HscB and IscS |
title_full | A New Tessera into the Interactome of the isc Operon: A Novel Interaction between HscB and IscS |
title_fullStr | A New Tessera into the Interactome of the isc Operon: A Novel Interaction between HscB and IscS |
title_full_unstemmed | A New Tessera into the Interactome of the isc Operon: A Novel Interaction between HscB and IscS |
title_short | A New Tessera into the Interactome of the isc Operon: A Novel Interaction between HscB and IscS |
title_sort | new tessera into the interactome of the isc operon: a novel interaction between hscb and iscs |
topic | Molecular Biosciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5037179/ https://www.ncbi.nlm.nih.gov/pubmed/27730125 http://dx.doi.org/10.3389/fmolb.2016.00048 |
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