Segmentation strategy of de novo designed four-helical bundles expands protein oligomerization modalities for cell regulation
New protein assemblies can be introduced through the fusion of selected proteins with di/oligomerization domains, which interact specifically with their partners but not with other cellular proteins. Here the authors demonstrate that a single four-helical bundle protein can be segmented into several...
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Format: | Article |
Language: | English |
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Nature Portfolio
2023-04-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-023-37765-6 |
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author | Estera Merljak Benjamin Malovrh Roman Jerala |
author_facet | Estera Merljak Benjamin Malovrh Roman Jerala |
author_sort | Estera Merljak |
collection | DOAJ |
description | New protein assemblies can be introduced through the fusion of selected proteins with di/oligomerization domains, which interact specifically with their partners but not with other cellular proteins. Here the authors demonstrate that a single four-helical bundle protein can be segmented into several different parts, defining up to four interacting molecules for enzyme reconstitution, gene expression, or CAR-T cell regulation. |
first_indexed | 2024-04-09T18:52:45Z |
format | Article |
id | doaj.art-69a0226d902f4e7b91425b4e0e1e3b31 |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-04-09T18:52:45Z |
publishDate | 2023-04-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-69a0226d902f4e7b91425b4e0e1e3b312023-04-09T11:21:31ZengNature PortfolioNature Communications2041-17232023-04-0114111210.1038/s41467-023-37765-6Segmentation strategy of de novo designed four-helical bundles expands protein oligomerization modalities for cell regulationEstera Merljak0Benjamin Malovrh1Roman Jerala2Department of Synthetic Biology and Immunology, National Institute of ChemistryDepartment of Synthetic Biology and Immunology, National Institute of ChemistryDepartment of Synthetic Biology and Immunology, National Institute of ChemistryNew protein assemblies can be introduced through the fusion of selected proteins with di/oligomerization domains, which interact specifically with their partners but not with other cellular proteins. Here the authors demonstrate that a single four-helical bundle protein can be segmented into several different parts, defining up to four interacting molecules for enzyme reconstitution, gene expression, or CAR-T cell regulation.https://doi.org/10.1038/s41467-023-37765-6 |
spellingShingle | Estera Merljak Benjamin Malovrh Roman Jerala Segmentation strategy of de novo designed four-helical bundles expands protein oligomerization modalities for cell regulation Nature Communications |
title | Segmentation strategy of de novo designed four-helical bundles expands protein oligomerization modalities for cell regulation |
title_full | Segmentation strategy of de novo designed four-helical bundles expands protein oligomerization modalities for cell regulation |
title_fullStr | Segmentation strategy of de novo designed four-helical bundles expands protein oligomerization modalities for cell regulation |
title_full_unstemmed | Segmentation strategy of de novo designed four-helical bundles expands protein oligomerization modalities for cell regulation |
title_short | Segmentation strategy of de novo designed four-helical bundles expands protein oligomerization modalities for cell regulation |
title_sort | segmentation strategy of de novo designed four helical bundles expands protein oligomerization modalities for cell regulation |
url | https://doi.org/10.1038/s41467-023-37765-6 |
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