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Deciphering peculiar protein-protein interacting modules in Deinococcus radiodurans

Interactomes of proteins under positive selection from ionizing-radiation-resistant bacteria (IRRB) might be a part of the answer to the question as to how IRRB, particularly Deinococcus radiodurans R(1 )(Deira), resist ionizing radiation. Here, using the Database of Interacting Proteins (DIP) and t...

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Detalles Bibliográficos
Autores principales: Mezhoud, Karim, Sghaier, Haïtham, Barkallah, Insaf
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2672081/
https://www.ncbi.nlm.nih.gov/pubmed/19356244
http://dx.doi.org/10.1186/1745-6150-4-12
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author Mezhoud, Karim
Sghaier, Haïtham
Barkallah, Insaf
author_facet Mezhoud, Karim
Sghaier, Haïtham
Barkallah, Insaf
author_sort Mezhoud, Karim
collection PubMed
description Interactomes of proteins under positive selection from ionizing-radiation-resistant bacteria (IRRB) might be a part of the answer to the question as to how IRRB, particularly Deinococcus radiodurans R(1 )(Deira), resist ionizing radiation. Here, using the Database of Interacting Proteins (DIP) and the Protein Structural Interactome (PSI)-base server for PSI map, we have predicted novel interactions of orthologs of the 58 proteins under positive selection in Deira and other IRRB, but which are absent in IRSB. Among these, 18 domains and their interactomes have been identified in DNA checkpoint and repair; kinases pathways; energy and nucleotide metabolisms were the important biological processes that were found to be involved. This finding provides new clues to the cellular pathways that can to be important for ionizing-radiation resistance in Deira.
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spelling pubmed-26720812009-04-23 Deciphering peculiar protein-protein interacting modules in Deinococcus radiodurans Mezhoud, Karim Sghaier, Haïtham Barkallah, Insaf Biol Direct Discovery Notes Interactomes of proteins under positive selection from ionizing-radiation-resistant bacteria (IRRB) might be a part of the answer to the question as to how IRRB, particularly Deinococcus radiodurans R(1 )(Deira), resist ionizing radiation. Here, using the Database of Interacting Proteins (DIP) and the Protein Structural Interactome (PSI)-base server for PSI map, we have predicted novel interactions of orthologs of the 58 proteins under positive selection in Deira and other IRRB, but which are absent in IRSB. Among these, 18 domains and their interactomes have been identified in DNA checkpoint and repair; kinases pathways; energy and nucleotide metabolisms were the important biological processes that were found to be involved. This finding provides new clues to the cellular pathways that can to be important for ionizing-radiation resistance in Deira. BioMed Central 2009-04-08 /pmc/articles/PMC2672081/ /pubmed/19356244 http://dx.doi.org/10.1186/1745-6150-4-12 Text en Copyright © 2009 Mezhoud et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Discovery Notes
Mezhoud, Karim
Sghaier, Haïtham
Barkallah, Insaf
Deciphering peculiar protein-protein interacting modules in Deinococcus radiodurans
title Deciphering peculiar protein-protein interacting modules in Deinococcus radiodurans
title_full Deciphering peculiar protein-protein interacting modules in Deinococcus radiodurans
title_fullStr Deciphering peculiar protein-protein interacting modules in Deinococcus radiodurans
title_full_unstemmed Deciphering peculiar protein-protein interacting modules in Deinococcus radiodurans
title_short Deciphering peculiar protein-protein interacting modules in Deinococcus radiodurans
title_sort deciphering peculiar protein-protein interacting modules in deinococcus radiodurans
topic Discovery Notes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2672081/
https://www.ncbi.nlm.nih.gov/pubmed/19356244
http://dx.doi.org/10.1186/1745-6150-4-12
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