Prioritizing targets for structural biology through the lens of proteomics: The archaeal protein TGAM_1934 from Thermococcus gammatolerans
ORFans are hypothetical proteins lacking any significant sequence similarity with other proteins. Here, we highlighted by quantitative proteomics the TGAM_1934 ORFan from the hyperradioresistant Thermococcus gammatolerans archaeon as one of the most abundant hypothetical proteins. This protein has been selected as a priority target for structure determination on the basis of its abundance in three cellular conditions. Its solution structure has been determined using multidimensional heteronuclear NMR spectroscopy. TGAM_1934 displays an original fold, although sharing some similarities with the 3D structure of the bacterial ortholog of frataxin, CyaY, a protein conserved in bacteria and eukaryotes and involved in iron–sulfur cluster biogenesis. These results highlight the potential of structural proteomics in prioritizing ORFan targets for structure determination based on quantitative proteomics data. The proteomic data and structure coordinates have been deposited to the ProteomeXchange with identifier PXD000402 (http://proteomecentral.proteomexchange.org/dataset/PXD000402) and Protein Data Bank under the accession number 2mcf, respectively.
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Subjects: | spectroscopie RMN, protéine, protéine bactérienne, protéomique quantitative, Bacteria, http://aims.fao.org/aos/agrovoc/c_24405, http://aims.fao.org/aos/agrovoc/c_6259, http://aims.fao.org/aos/agrovoc/c_24141, http://aims.fao.org/aos/agrovoc/c_61d06119, http://aims.fao.org/aos/agrovoc/c_765, http://aims.fao.org/aos/agrovoc/c_3081, |
Online Access: | http://agritrop.cirad.fr/600068/ http://agritrop.cirad.fr/600068/1/2015%20Proteomics%20-%202014%20-%20Yang%20-%20Prioritizing%20targets%20for%20structural%20biology%20through%20the%20lens%20of%20proteomics%20%20The%20archaeal%20protein%20%281%29.pdf |
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dig-cirad-fr-6000682024-01-29T05:45:10Z http://agritrop.cirad.fr/600068/ http://agritrop.cirad.fr/600068/ Prioritizing targets for structural biology through the lens of proteomics: The archaeal protein TGAM_1934 from Thermococcus gammatolerans. Yang Yin-Shan, Fernandez Bernard, Lagorce Arnaud, Aloin Valérie, Montet De Guillen Karine, Boyer Jean-Baptiste, Dedieu Alain, Confalonieri Fabrice, Armengaud Jean, Roumestand Christian. 2015. Proteomics, 15 (1) : 114-123.https://doi.org/10.1002/pmic.201300535 <https://doi.org/10.1002/pmic.201300535> Prioritizing targets for structural biology through the lens of proteomics: The archaeal protein TGAM_1934 from Thermococcus gammatolerans Yang, Yin-Shan Fernandez, Bernard Lagorce, Arnaud Aloin, Valérie Montet De Guillen, Karine Boyer, Jean-Baptiste Dedieu, Alain Confalonieri, Fabrice Armengaud, Jean Roumestand, Christian eng 2015 Proteomics spectroscopie RMN protéine protéine bactérienne protéomique quantitative Bacteria http://aims.fao.org/aos/agrovoc/c_24405 http://aims.fao.org/aos/agrovoc/c_6259 http://aims.fao.org/aos/agrovoc/c_24141 http://aims.fao.org/aos/agrovoc/c_61d06119 http://aims.fao.org/aos/agrovoc/c_765 France http://aims.fao.org/aos/agrovoc/c_3081 ORFans are hypothetical proteins lacking any significant sequence similarity with other proteins. Here, we highlighted by quantitative proteomics the TGAM_1934 ORFan from the hyperradioresistant Thermococcus gammatolerans archaeon as one of the most abundant hypothetical proteins. This protein has been selected as a priority target for structure determination on the basis of its abundance in three cellular conditions. Its solution structure has been determined using multidimensional heteronuclear NMR spectroscopy. TGAM_1934 displays an original fold, although sharing some similarities with the 3D structure of the bacterial ortholog of frataxin, CyaY, a protein conserved in bacteria and eukaryotes and involved in iron–sulfur cluster biogenesis. These results highlight the potential of structural proteomics in prioritizing ORFan targets for structure determination based on quantitative proteomics data. The proteomic data and structure coordinates have been deposited to the ProteomeXchange with identifier PXD000402 (http://proteomecentral.proteomexchange.org/dataset/PXD000402) and Protein Data Bank under the accession number 2mcf, respectively. article info:eu-repo/semantics/article Journal Article info:eu-repo/semantics/publishedVersion http://agritrop.cirad.fr/600068/1/2015%20Proteomics%20-%202014%20-%20Yang%20-%20Prioritizing%20targets%20for%20structural%20biology%20through%20the%20lens%20of%20proteomics%20%20The%20archaeal%20protein%20%281%29.pdf text Cirad license info:eu-repo/semantics/restrictedAccess https://agritrop.cirad.fr/mention_legale.html https://doi.org/10.1002/pmic.201300535 10.1002/pmic.201300535 info:eu-repo/semantics/altIdentifier/doi/10.1002/pmic.201300535 info:eu-repo/semantics/altIdentifier/purl/https://doi.org/10.1002/pmic.201300535 info:eu-repo/semantics/dataset/purl/https://doi.org/10.6019/PXD000402 |
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spectroscopie RMN protéine protéine bactérienne protéomique quantitative Bacteria http://aims.fao.org/aos/agrovoc/c_24405 http://aims.fao.org/aos/agrovoc/c_6259 http://aims.fao.org/aos/agrovoc/c_24141 http://aims.fao.org/aos/agrovoc/c_61d06119 http://aims.fao.org/aos/agrovoc/c_765 http://aims.fao.org/aos/agrovoc/c_3081 spectroscopie RMN protéine protéine bactérienne protéomique quantitative Bacteria http://aims.fao.org/aos/agrovoc/c_24405 http://aims.fao.org/aos/agrovoc/c_6259 http://aims.fao.org/aos/agrovoc/c_24141 http://aims.fao.org/aos/agrovoc/c_61d06119 http://aims.fao.org/aos/agrovoc/c_765 http://aims.fao.org/aos/agrovoc/c_3081 |
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spectroscopie RMN protéine protéine bactérienne protéomique quantitative Bacteria http://aims.fao.org/aos/agrovoc/c_24405 http://aims.fao.org/aos/agrovoc/c_6259 http://aims.fao.org/aos/agrovoc/c_24141 http://aims.fao.org/aos/agrovoc/c_61d06119 http://aims.fao.org/aos/agrovoc/c_765 http://aims.fao.org/aos/agrovoc/c_3081 spectroscopie RMN protéine protéine bactérienne protéomique quantitative Bacteria http://aims.fao.org/aos/agrovoc/c_24405 http://aims.fao.org/aos/agrovoc/c_6259 http://aims.fao.org/aos/agrovoc/c_24141 http://aims.fao.org/aos/agrovoc/c_61d06119 http://aims.fao.org/aos/agrovoc/c_765 http://aims.fao.org/aos/agrovoc/c_3081 Yang, Yin-Shan Fernandez, Bernard Lagorce, Arnaud Aloin, Valérie Montet De Guillen, Karine Boyer, Jean-Baptiste Dedieu, Alain Confalonieri, Fabrice Armengaud, Jean Roumestand, Christian Prioritizing targets for structural biology through the lens of proteomics: The archaeal protein TGAM_1934 from Thermococcus gammatolerans |
description |
ORFans are hypothetical proteins lacking any significant sequence similarity with other proteins. Here, we highlighted by quantitative proteomics the TGAM_1934 ORFan from the hyperradioresistant Thermococcus gammatolerans archaeon as one of the most abundant hypothetical proteins. This protein has been selected as a priority target for structure determination on the basis of its abundance in three cellular conditions. Its solution structure has been determined using multidimensional heteronuclear NMR spectroscopy. TGAM_1934 displays an original fold, although sharing some similarities with the 3D structure of the bacterial ortholog of frataxin, CyaY, a protein conserved in bacteria and eukaryotes and involved in iron–sulfur cluster biogenesis. These results highlight the potential of structural proteomics in prioritizing ORFan targets for structure determination based on quantitative proteomics data. The proteomic data and structure coordinates have been deposited to the ProteomeXchange with identifier PXD000402 (http://proteomecentral.proteomexchange.org/dataset/PXD000402) and Protein Data Bank under the accession number 2mcf, respectively. |
format |
article |
topic_facet |
spectroscopie RMN protéine protéine bactérienne protéomique quantitative Bacteria http://aims.fao.org/aos/agrovoc/c_24405 http://aims.fao.org/aos/agrovoc/c_6259 http://aims.fao.org/aos/agrovoc/c_24141 http://aims.fao.org/aos/agrovoc/c_61d06119 http://aims.fao.org/aos/agrovoc/c_765 http://aims.fao.org/aos/agrovoc/c_3081 |
author |
Yang, Yin-Shan Fernandez, Bernard Lagorce, Arnaud Aloin, Valérie Montet De Guillen, Karine Boyer, Jean-Baptiste Dedieu, Alain Confalonieri, Fabrice Armengaud, Jean Roumestand, Christian |
author_facet |
Yang, Yin-Shan Fernandez, Bernard Lagorce, Arnaud Aloin, Valérie Montet De Guillen, Karine Boyer, Jean-Baptiste Dedieu, Alain Confalonieri, Fabrice Armengaud, Jean Roumestand, Christian |
author_sort |
Yang, Yin-Shan |
title |
Prioritizing targets for structural biology through the lens of proteomics: The archaeal protein TGAM_1934 from Thermococcus gammatolerans |
title_short |
Prioritizing targets for structural biology through the lens of proteomics: The archaeal protein TGAM_1934 from Thermococcus gammatolerans |
title_full |
Prioritizing targets for structural biology through the lens of proteomics: The archaeal protein TGAM_1934 from Thermococcus gammatolerans |
title_fullStr |
Prioritizing targets for structural biology through the lens of proteomics: The archaeal protein TGAM_1934 from Thermococcus gammatolerans |
title_full_unstemmed |
Prioritizing targets for structural biology through the lens of proteomics: The archaeal protein TGAM_1934 from Thermococcus gammatolerans |
title_sort |
prioritizing targets for structural biology through the lens of proteomics: the archaeal protein tgam_1934 from thermococcus gammatolerans |
url |
http://agritrop.cirad.fr/600068/ http://agritrop.cirad.fr/600068/1/2015%20Proteomics%20-%202014%20-%20Yang%20-%20Prioritizing%20targets%20for%20structural%20biology%20through%20the%20lens%20of%20proteomics%20%20The%20archaeal%20protein%20%281%29.pdf |
work_keys_str_mv |
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