A comprehensive resource of interacting protein regions for refining human transcription factor networks.

Large-scale data sets of protein-protein interactions (PPIs) are a valuable resource for mapping and analysis of the topological and dynamic features of interactome networks. The currently available large-scale PPI data sets only contain information on interaction partners. The data presented in thi...

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Autores principales: Etsuko Miyamoto-Sato, Shigeo Fujimori, Masamichi Ishizaka, Naoya Hirai, Kazuyo Masuoka, Rintaro Saito, Yosuke Ozawa, Katsuya Hino, Takanori Washio, Masaru Tomita, Tatsuhiro Yamashita, Tomohiro Oshikubo, Hidetoshi Akasaka, Jun Sugiyama, Yasuo Matsumoto, Hiroshi Yanagawa
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Publicado: Public Library of Science (PLoS) 2010
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spelling oai:doaj.org-article:7f9bc5798d2f455a8dcf1af2ea640e542021-11-25T06:25:36ZA comprehensive resource of interacting protein regions for refining human transcription factor networks.1932-620310.1371/journal.pone.0009289https://doaj.org/article/7f9bc5798d2f455a8dcf1af2ea640e542010-02-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20195357/?tool=EBIhttps://doaj.org/toc/1932-6203Large-scale data sets of protein-protein interactions (PPIs) are a valuable resource for mapping and analysis of the topological and dynamic features of interactome networks. The currently available large-scale PPI data sets only contain information on interaction partners. The data presented in this study also include the sequences involved in the interactions (i.e., the interacting regions, IRs) suggested to correspond to functional and structural domains. Here we present the first large-scale IR data set obtained using mRNA display for 50 human transcription factors (TFs), including 12 transcription-related proteins. The core data set (966 IRs; 943 PPIs) displays a verification rate of 70%. Analysis of the IR data set revealed the existence of IRs that interact with multiple partners. Furthermore, these IRs were preferentially associated with intrinsic disorder. This finding supports the hypothesis that intrinsically disordered regions play a major role in the dynamics and diversity of TF networks through their ability to structurally adapt to and bind with multiple partners. Accordingly, this domain-based interaction resource represents an important step in refining protein interactions and networks at the domain level and in associating network analysis with biological structure and function.Etsuko Miyamoto-SatoShigeo FujimoriMasamichi IshizakaNaoya HiraiKazuyo MasuokaRintaro SaitoYosuke OzawaKatsuya HinoTakanori WashioMasaru TomitaTatsuhiro YamashitaTomohiro OshikuboHidetoshi AkasakaJun SugiyamaYasuo MatsumotoHiroshi YanagawaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 2, p e9289 (2010)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Etsuko Miyamoto-Sato
Shigeo Fujimori
Masamichi Ishizaka
Naoya Hirai
Kazuyo Masuoka
Rintaro Saito
Yosuke Ozawa
Katsuya Hino
Takanori Washio
Masaru Tomita
Tatsuhiro Yamashita
Tomohiro Oshikubo
Hidetoshi Akasaka
Jun Sugiyama
Yasuo Matsumoto
Hiroshi Yanagawa
A comprehensive resource of interacting protein regions for refining human transcription factor networks.
description Large-scale data sets of protein-protein interactions (PPIs) are a valuable resource for mapping and analysis of the topological and dynamic features of interactome networks. The currently available large-scale PPI data sets only contain information on interaction partners. The data presented in this study also include the sequences involved in the interactions (i.e., the interacting regions, IRs) suggested to correspond to functional and structural domains. Here we present the first large-scale IR data set obtained using mRNA display for 50 human transcription factors (TFs), including 12 transcription-related proteins. The core data set (966 IRs; 943 PPIs) displays a verification rate of 70%. Analysis of the IR data set revealed the existence of IRs that interact with multiple partners. Furthermore, these IRs were preferentially associated with intrinsic disorder. This finding supports the hypothesis that intrinsically disordered regions play a major role in the dynamics and diversity of TF networks through their ability to structurally adapt to and bind with multiple partners. Accordingly, this domain-based interaction resource represents an important step in refining protein interactions and networks at the domain level and in associating network analysis with biological structure and function.
format article
author Etsuko Miyamoto-Sato
Shigeo Fujimori
Masamichi Ishizaka
Naoya Hirai
Kazuyo Masuoka
Rintaro Saito
Yosuke Ozawa
Katsuya Hino
Takanori Washio
Masaru Tomita
Tatsuhiro Yamashita
Tomohiro Oshikubo
Hidetoshi Akasaka
Jun Sugiyama
Yasuo Matsumoto
Hiroshi Yanagawa
author_facet Etsuko Miyamoto-Sato
Shigeo Fujimori
Masamichi Ishizaka
Naoya Hirai
Kazuyo Masuoka
Rintaro Saito
Yosuke Ozawa
Katsuya Hino
Takanori Washio
Masaru Tomita
Tatsuhiro Yamashita
Tomohiro Oshikubo
Hidetoshi Akasaka
Jun Sugiyama
Yasuo Matsumoto
Hiroshi Yanagawa
author_sort Etsuko Miyamoto-Sato
title A comprehensive resource of interacting protein regions for refining human transcription factor networks.
title_short A comprehensive resource of interacting protein regions for refining human transcription factor networks.
title_full A comprehensive resource of interacting protein regions for refining human transcription factor networks.
title_fullStr A comprehensive resource of interacting protein regions for refining human transcription factor networks.
title_full_unstemmed A comprehensive resource of interacting protein regions for refining human transcription factor networks.
title_sort comprehensive resource of interacting protein regions for refining human transcription factor networks.
publisher Public Library of Science (PLoS)
publishDate 2010
url https://doaj.org/article/7f9bc5798d2f455a8dcf1af2ea640e54
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