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A new principle of oligomerization of plant DEG7 protease based on interactions of degenerated protease domains
Deg/HtrA proteases are a large group of ATP-independent serine endoproteases found in almost every organism. Their usual domain arrangement comprises a trypsin-type protease domain and one or more PDZ domains. All Deg/HtrA proteases form homo-oligomers with trimers as the basic unit, where the activ...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3194040/ https://www.ncbi.nlm.nih.gov/pubmed/21247409 http://dx.doi.org/10.1042/BJ20101613 |
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author | Schuhmann, Holger Mogg, Ulrike Adamska, Iwona |
author_facet | Schuhmann, Holger Mogg, Ulrike Adamska, Iwona |
author_sort | Schuhmann, Holger |
collection | PubMed |
description | Deg/HtrA proteases are a large group of ATP-independent serine endoproteases found in almost every organism. Their usual domain arrangement comprises a trypsin-type protease domain and one or more PDZ domains. All Deg/HtrA proteases form homo-oligomers with trimers as the basic unit, where the active protease domain mediates the interaction between individual monomers. Among the members of the Deg/HtrA protease family, the plant protease DEG7 is unique since it contains two protease domains (one active and one degenerated) and four PDZ domains. In the present study, we investigated the oligomerization behaviour of this unusual protease using yeast two-hybrid analysis in vivo and with recombinant protein in vitro. We show that DEG7 forms trimeric complexes, but in contrast with other known Deg/HtrA proteases, it shows a new principle of oligomerization, where trimerization is based on the interactions between degenerated protease domains. We propose that, during evolution, a duplicated active protease domain degenerated and specialized in protein–protein interaction and complex formation. |
format | Online Article Text |
id | pubmed-3194040 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-31940402011-12-23 A new principle of oligomerization of plant DEG7 protease based on interactions of degenerated protease domains Schuhmann, Holger Mogg, Ulrike Adamska, Iwona Biochem J Research Article Deg/HtrA proteases are a large group of ATP-independent serine endoproteases found in almost every organism. Their usual domain arrangement comprises a trypsin-type protease domain and one or more PDZ domains. All Deg/HtrA proteases form homo-oligomers with trimers as the basic unit, where the active protease domain mediates the interaction between individual monomers. Among the members of the Deg/HtrA protease family, the plant protease DEG7 is unique since it contains two protease domains (one active and one degenerated) and four PDZ domains. In the present study, we investigated the oligomerization behaviour of this unusual protease using yeast two-hybrid analysis in vivo and with recombinant protein in vitro. We show that DEG7 forms trimeric complexes, but in contrast with other known Deg/HtrA proteases, it shows a new principle of oligomerization, where trimerization is based on the interactions between degenerated protease domains. We propose that, during evolution, a duplicated active protease domain degenerated and specialized in protein–protein interaction and complex formation. Portland Press Ltd. 2011-03-15 2011-04-01 /pmc/articles/PMC3194040/ /pubmed/21247409 http://dx.doi.org/10.1042/BJ20101613 Text en © 2011 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited. http://creativecommons.org/licenses/by-nc/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Schuhmann, Holger Mogg, Ulrike Adamska, Iwona A new principle of oligomerization of plant DEG7 protease based on interactions of degenerated protease domains |
title | A new principle of oligomerization of plant DEG7 protease based on interactions of degenerated protease domains |
title_full | A new principle of oligomerization of plant DEG7 protease based on interactions of degenerated protease domains |
title_fullStr | A new principle of oligomerization of plant DEG7 protease based on interactions of degenerated protease domains |
title_full_unstemmed | A new principle of oligomerization of plant DEG7 protease based on interactions of degenerated protease domains |
title_short | A new principle of oligomerization of plant DEG7 protease based on interactions of degenerated protease domains |
title_sort | new principle of oligomerization of plant deg7 protease based on interactions of degenerated protease domains |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3194040/ https://www.ncbi.nlm.nih.gov/pubmed/21247409 http://dx.doi.org/10.1042/BJ20101613 |
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