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Fairy “tails”: flexibility and function of intrinsically disordered extensions in the photosynthetic world

Intrinsically Disordered Proteins (IDPs), or protein fragments also called Intrinsically Disordered Regions (IDRs), display high flexibility as the result of their amino acid composition. They can adopt multiple roles. In globular proteins, IDRs are usually found as loops and linkers between seconda...

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Autores principales: Thieulin-Pardo, Gabriel, Avilan, Luisana, Kojadinovic, Mila, Gontero, Brigitte
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4436894/
https://www.ncbi.nlm.nih.gov/pubmed/26042223
http://dx.doi.org/10.3389/fmolb.2015.00023
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author Thieulin-Pardo, Gabriel
Avilan, Luisana
Kojadinovic, Mila
Gontero, Brigitte
author_facet Thieulin-Pardo, Gabriel
Avilan, Luisana
Kojadinovic, Mila
Gontero, Brigitte
author_sort Thieulin-Pardo, Gabriel
collection PubMed
description Intrinsically Disordered Proteins (IDPs), or protein fragments also called Intrinsically Disordered Regions (IDRs), display high flexibility as the result of their amino acid composition. They can adopt multiple roles. In globular proteins, IDRs are usually found as loops and linkers between secondary structure elements. However, not all disordered fragments are loops: some proteins bear an intrinsically disordered extension at their C- or N-terminus, and this flexibility can affect the protein as a whole. In this review, we focus on the disordered N- and C-terminal extensions of globular proteins from photosynthetic organisms. Using the examples of the A(2)B(2)-GAPDH and the α Rubisco activase isoform, we show that intrinsically disordered extensions can help regulate their “host” protein in response to changes in light, thereby participating in photosynthesis regulation. As IDPs are famous for their large number of protein partners, we used the examples of the NAC, bZIP, TCP, and GRAS transcription factor families to illustrate the fact that intrinsically disordered extremities can allow a protein to have an increased number of partners, which directly affects its regulation. Finally, for proteins from the cryptochrome light receptor family, we describe how a new role for the photolyase proteins may emerge by the addition of an intrinsically disordered extension, while still allowing the protein to absorb blue light. This review has highlighted the diverse repercussions of the disordered extension on the regulation and function of their host protein and outlined possible future research avenues.
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spelling pubmed-44368942015-06-03 Fairy “tails”: flexibility and function of intrinsically disordered extensions in the photosynthetic world Thieulin-Pardo, Gabriel Avilan, Luisana Kojadinovic, Mila Gontero, Brigitte Front Mol Biosci Molecular Biosciences Intrinsically Disordered Proteins (IDPs), or protein fragments also called Intrinsically Disordered Regions (IDRs), display high flexibility as the result of their amino acid composition. They can adopt multiple roles. In globular proteins, IDRs are usually found as loops and linkers between secondary structure elements. However, not all disordered fragments are loops: some proteins bear an intrinsically disordered extension at their C- or N-terminus, and this flexibility can affect the protein as a whole. In this review, we focus on the disordered N- and C-terminal extensions of globular proteins from photosynthetic organisms. Using the examples of the A(2)B(2)-GAPDH and the α Rubisco activase isoform, we show that intrinsically disordered extensions can help regulate their “host” protein in response to changes in light, thereby participating in photosynthesis regulation. As IDPs are famous for their large number of protein partners, we used the examples of the NAC, bZIP, TCP, and GRAS transcription factor families to illustrate the fact that intrinsically disordered extremities can allow a protein to have an increased number of partners, which directly affects its regulation. Finally, for proteins from the cryptochrome light receptor family, we describe how a new role for the photolyase proteins may emerge by the addition of an intrinsically disordered extension, while still allowing the protein to absorb blue light. This review has highlighted the diverse repercussions of the disordered extension on the regulation and function of their host protein and outlined possible future research avenues. Frontiers Media S.A. 2015-05-19 /pmc/articles/PMC4436894/ /pubmed/26042223 http://dx.doi.org/10.3389/fmolb.2015.00023 Text en Copyright © 2015 Thieulin-Pardo, Avilan, Kojadinovic and Gontero. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Molecular Biosciences
Thieulin-Pardo, Gabriel
Avilan, Luisana
Kojadinovic, Mila
Gontero, Brigitte
Fairy “tails”: flexibility and function of intrinsically disordered extensions in the photosynthetic world
title Fairy “tails”: flexibility and function of intrinsically disordered extensions in the photosynthetic world
title_full Fairy “tails”: flexibility and function of intrinsically disordered extensions in the photosynthetic world
title_fullStr Fairy “tails”: flexibility and function of intrinsically disordered extensions in the photosynthetic world
title_full_unstemmed Fairy “tails”: flexibility and function of intrinsically disordered extensions in the photosynthetic world
title_short Fairy “tails”: flexibility and function of intrinsically disordered extensions in the photosynthetic world
title_sort fairy “tails”: flexibility and function of intrinsically disordered extensions in the photosynthetic world
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4436894/
https://www.ncbi.nlm.nih.gov/pubmed/26042223
http://dx.doi.org/10.3389/fmolb.2015.00023
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