A novel mode of interaction between intrinsically disordered proteins
An increasing number of proteins, which have neither regular secondary nor well-defined tertiary structures, have been found to be present in cells. The structure of these proteins is highly flexible and disordered under physiological (native) conditions, and they are called “intrinsically disordere...
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The Biophysical Society of Japan
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Online Access: | https://doi.org/10.2142/biophysico.BSJ-2020012 |
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doaj-170f337bb330485eb9128eb9e842c4342020-11-25T03:07:22ZengThe Biophysical Society of JapanBiophysics and Physicobiology2189-47792020-08-011710.2142/biophysico.BSJ-2020012A novel mode of interaction between intrinsically disordered proteinsEmi Hibino0Masaru Hoshino1Graduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, Aichi 464-8601, JapanGraduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, JapanAn increasing number of proteins, which have neither regular secondary nor well-defined tertiary structures, have been found to be present in cells. The structure of these proteins is highly flexible and disordered under physiological (native) conditions, and they are called “intrinsically disordered” proteins (IDPs). Many of the IDPs are involved in interactions with other biomolecules such as DNA, RNA, carbohydrates, and proteins. While these IDPs are largely unstructured by themselves, marked conformational changes often occur upon binding to an interacting partner, which is known as the “coupled folding and binding mechanism”, which enable them to change the conformation to become compatible with the shape of the multiple target biomolecules. We have studied the structure and interaction of eukaryotic transcription factors Sp1 and TAF4, and found that both of them have long intrinsically disordered regions (IDRs). One of the IDRs in Sp1 exhibited homo-oligomer formation. In addition, the same region was used for the interaction with another IDR found in the TAF4 molecule. In both cases, we have not detected any significant conformational change in that region, suggesting a prominent and novel binding mode for IDPs/IDRs, which are not categorized by the well-accepted concept of the coupled folding and binding mechanism.https://doi.org/10.2142/biophysico.BSJ-2020012protein-protein interactionconformational changecoupled folding and bindingnuclear magnetic resonancetranscription factor |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Emi Hibino Masaru Hoshino |
spellingShingle |
Emi Hibino Masaru Hoshino A novel mode of interaction between intrinsically disordered proteins Biophysics and Physicobiology protein-protein interaction conformational change coupled folding and binding nuclear magnetic resonance transcription factor |
author_facet |
Emi Hibino Masaru Hoshino |
author_sort |
Emi Hibino |
title |
A novel mode of interaction between intrinsically disordered proteins |
title_short |
A novel mode of interaction between intrinsically disordered proteins |
title_full |
A novel mode of interaction between intrinsically disordered proteins |
title_fullStr |
A novel mode of interaction between intrinsically disordered proteins |
title_full_unstemmed |
A novel mode of interaction between intrinsically disordered proteins |
title_sort |
novel mode of interaction between intrinsically disordered proteins |
publisher |
The Biophysical Society of Japan |
series |
Biophysics and Physicobiology |
issn |
2189-4779 |
publishDate |
2020-08-01 |
description |
An increasing number of proteins, which have neither regular secondary nor well-defined tertiary structures, have been found to be present in cells. The structure of these proteins is highly flexible and disordered under physiological (native) conditions, and they are called “intrinsically disordered” proteins (IDPs). Many of the IDPs are involved in interactions with other biomolecules such as DNA, RNA, carbohydrates, and proteins. While these IDPs are largely unstructured by themselves, marked conformational changes often occur upon binding to an interacting partner, which is known as the “coupled folding and binding mechanism”, which enable them to change the conformation to become compatible with the shape of the multiple target biomolecules. We have studied the structure and interaction of eukaryotic transcription factors Sp1 and TAF4, and found that both of them have long intrinsically disordered regions (IDRs). One of the IDRs in Sp1 exhibited homo-oligomer formation. In addition, the same region was used for the interaction with another IDR found in the TAF4 molecule. In both cases, we have not detected any significant conformational change in that region, suggesting a prominent and novel binding mode for IDPs/IDRs, which are not categorized by the well-accepted concept of the coupled folding and binding mechanism. |
topic |
protein-protein interaction conformational change coupled folding and binding nuclear magnetic resonance transcription factor |
url |
https://doi.org/10.2142/biophysico.BSJ-2020012 |
work_keys_str_mv |
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