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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Main Authors: Yang, Yin-Shan, Fernandez, Bernard, Lagorce, Arnaud, Aloin, Valérie, Montet De Guillen, Karine, Boyer, Jean-Baptiste, Dedieu, Alain, Confalonieri, Fabrice, Armengaud, Jean, Roumestand, Christian
Format: article biblioteca
Language:eng
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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spelling 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
institution CIRAD FR
collection DSpace
country Francia
countrycode FR
component Bibliográfico
access En linea
databasecode dig-cirad-fr
tag biblioteca
region Europa del Oeste
libraryname Biblioteca del CIRAD Francia
language eng
topic 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
spellingShingle 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
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