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The role of peptide motifs in the evolution of a protein network
Naturally occurring proteins in cellular networks often share peptide motifs. These motifs have been known to play a pivotal role in protein interactions among the components of a network. However, it remains unknown how these motifs have contributed to the evolution of the protein network. Here we...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2095796/ https://www.ncbi.nlm.nih.gov/pubmed/17881369 http://dx.doi.org/10.1093/nar/gkm692 |
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author | Saito, Hirohide Kashida, Shunnichi Inoue, Tan Shiba, Kiyotaka |
author_facet | Saito, Hirohide Kashida, Shunnichi Inoue, Tan Shiba, Kiyotaka |
author_sort | Saito, Hirohide |
collection | PubMed |
description | Naturally occurring proteins in cellular networks often share peptide motifs. These motifs have been known to play a pivotal role in protein interactions among the components of a network. However, it remains unknown how these motifs have contributed to the evolution of the protein network. Here we addressed this issue by a synthetic biology approach. Through the motif programming method, we have constructed an artificial protein library by mixing four peptide motifs shared among the Bcl-2 family proteins that positively or negatively regulate the apoptosis networks. We found one strong pro-apoptotic protein, d29, and two proteins having moderate, but unambiguous anti-apoptotic functions, a10 and d16, from the 28 tested clones. Thus both the pro- and anti-apoptotic modulators were present in the library, demonstrating that functional proteins with opposing effects can emerge from a single pool prepared from common motifs. Motif programming studies have exhibited that the annotated function of the motifs were significantly influenced by the context that the motifs embedded. The results further revealed that reshuffling of a set of motifs realized the promiscuous state of protein, from which disparate functions could emerge. Our finding suggests that motifs contributed to the plastic evolvability of the protein network. |
format | Text |
id | pubmed-2095796 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-20957962007-12-07 The role of peptide motifs in the evolution of a protein network Saito, Hirohide Kashida, Shunnichi Inoue, Tan Shiba, Kiyotaka Nucleic Acids Res Molecular Biology Naturally occurring proteins in cellular networks often share peptide motifs. These motifs have been known to play a pivotal role in protein interactions among the components of a network. However, it remains unknown how these motifs have contributed to the evolution of the protein network. Here we addressed this issue by a synthetic biology approach. Through the motif programming method, we have constructed an artificial protein library by mixing four peptide motifs shared among the Bcl-2 family proteins that positively or negatively regulate the apoptosis networks. We found one strong pro-apoptotic protein, d29, and two proteins having moderate, but unambiguous anti-apoptotic functions, a10 and d16, from the 28 tested clones. Thus both the pro- and anti-apoptotic modulators were present in the library, demonstrating that functional proteins with opposing effects can emerge from a single pool prepared from common motifs. Motif programming studies have exhibited that the annotated function of the motifs were significantly influenced by the context that the motifs embedded. The results further revealed that reshuffling of a set of motifs realized the promiscuous state of protein, from which disparate functions could emerge. Our finding suggests that motifs contributed to the plastic evolvability of the protein network. Oxford University Press 2007-10 2007-09-18 /pmc/articles/PMC2095796/ /pubmed/17881369 http://dx.doi.org/10.1093/nar/gkm692 Text en © 2007 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Molecular Biology Saito, Hirohide Kashida, Shunnichi Inoue, Tan Shiba, Kiyotaka The role of peptide motifs in the evolution of a protein network |
title | The role of peptide motifs in the evolution of a protein network |
title_full | The role of peptide motifs in the evolution of a protein network |
title_fullStr | The role of peptide motifs in the evolution of a protein network |
title_full_unstemmed | The role of peptide motifs in the evolution of a protein network |
title_short | The role of peptide motifs in the evolution of a protein network |
title_sort | role of peptide motifs in the evolution of a protein network |
topic | Molecular Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2095796/ https://www.ncbi.nlm.nih.gov/pubmed/17881369 http://dx.doi.org/10.1093/nar/gkm692 |
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