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KORRIGAN1 Interacts Specifically with Integral Components of the Cellulose Synthase Machinery

Cellulose is synthesized by the so called rosette protein complex and the catalytic subunits of this complex are the cellulose synthases (CESAs). It is thought that the rosette complexes in the primary and secondary cell walls each contains at least three different non-redundant cellulose synthases....

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Autores principales: Mansoori, Nasim, Timmers, Jaap, Desprez, Thierry, Kamei, Claire L. A., Dees, Dianka C. T., Vincken, Jean-Paul, Visser, Richard G. F., Höfte, Herman, Vernhettes, Samantha, Trindade, Luisa M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4226561/
https://www.ncbi.nlm.nih.gov/pubmed/25383767
http://dx.doi.org/10.1371/journal.pone.0112387
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author Mansoori, Nasim
Timmers, Jaap
Desprez, Thierry
Kamei, Claire L. A.
Dees, Dianka C. T.
Vincken, Jean-Paul
Visser, Richard G. F.
Höfte, Herman
Vernhettes, Samantha
Trindade, Luisa M.
author_facet Mansoori, Nasim
Timmers, Jaap
Desprez, Thierry
Kamei, Claire L. A.
Dees, Dianka C. T.
Vincken, Jean-Paul
Visser, Richard G. F.
Höfte, Herman
Vernhettes, Samantha
Trindade, Luisa M.
author_sort Mansoori, Nasim
collection PubMed
description Cellulose is synthesized by the so called rosette protein complex and the catalytic subunits of this complex are the cellulose synthases (CESAs). It is thought that the rosette complexes in the primary and secondary cell walls each contains at least three different non-redundant cellulose synthases. In addition to the CESA proteins, cellulose biosynthesis almost certainly requires the action of other proteins, although few have been identified and little is known about the biochemical role of those that have been identified. One of these proteins is KORRIGAN (KOR1). Mutant analysis of this protein in Arabidopsis thaliana showed altered cellulose content in both the primary and secondary cell wall. KOR1 is thought to be required for cellulose synthesis acting as a cellulase at the plasma membrane–cell wall interface. KOR1 has recently been shown to interact with the primary cellulose synthase rosette complex however direct interaction with that of the secondary cell wall has never been demonstrated. Using various methods, both in vitro and in planta, it was shown that KOR1 interacts specifically with only two of the secondary CESA proteins. The KOR1 protein domain(s) involved in the interaction with the CESA proteins were also identified by analyzing the interaction of truncated forms of KOR1 with CESA proteins. The KOR1 transmembrane domain has shown to be required for the interaction between KOR1 and the different CESAs, as well as for higher oligomer formation of KOR1.
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spelling pubmed-42265612014-11-13 KORRIGAN1 Interacts Specifically with Integral Components of the Cellulose Synthase Machinery Mansoori, Nasim Timmers, Jaap Desprez, Thierry Kamei, Claire L. A. Dees, Dianka C. T. Vincken, Jean-Paul Visser, Richard G. F. Höfte, Herman Vernhettes, Samantha Trindade, Luisa M. PLoS One Research Article Cellulose is synthesized by the so called rosette protein complex and the catalytic subunits of this complex are the cellulose synthases (CESAs). It is thought that the rosette complexes in the primary and secondary cell walls each contains at least three different non-redundant cellulose synthases. In addition to the CESA proteins, cellulose biosynthesis almost certainly requires the action of other proteins, although few have been identified and little is known about the biochemical role of those that have been identified. One of these proteins is KORRIGAN (KOR1). Mutant analysis of this protein in Arabidopsis thaliana showed altered cellulose content in both the primary and secondary cell wall. KOR1 is thought to be required for cellulose synthesis acting as a cellulase at the plasma membrane–cell wall interface. KOR1 has recently been shown to interact with the primary cellulose synthase rosette complex however direct interaction with that of the secondary cell wall has never been demonstrated. Using various methods, both in vitro and in planta, it was shown that KOR1 interacts specifically with only two of the secondary CESA proteins. The KOR1 protein domain(s) involved in the interaction with the CESA proteins were also identified by analyzing the interaction of truncated forms of KOR1 with CESA proteins. The KOR1 transmembrane domain has shown to be required for the interaction between KOR1 and the different CESAs, as well as for higher oligomer formation of KOR1. Public Library of Science 2014-11-10 /pmc/articles/PMC4226561/ /pubmed/25383767 http://dx.doi.org/10.1371/journal.pone.0112387 Text en © 2014 Mansoori et al http://creativecommons.org/licenses/by/4.0/ 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 author and source are properly credited.
spellingShingle Research Article
Mansoori, Nasim
Timmers, Jaap
Desprez, Thierry
Kamei, Claire L. A.
Dees, Dianka C. T.
Vincken, Jean-Paul
Visser, Richard G. F.
Höfte, Herman
Vernhettes, Samantha
Trindade, Luisa M.
KORRIGAN1 Interacts Specifically with Integral Components of the Cellulose Synthase Machinery
title KORRIGAN1 Interacts Specifically with Integral Components of the Cellulose Synthase Machinery
title_full KORRIGAN1 Interacts Specifically with Integral Components of the Cellulose Synthase Machinery
title_fullStr KORRIGAN1 Interacts Specifically with Integral Components of the Cellulose Synthase Machinery
title_full_unstemmed KORRIGAN1 Interacts Specifically with Integral Components of the Cellulose Synthase Machinery
title_short KORRIGAN1 Interacts Specifically with Integral Components of the Cellulose Synthase Machinery
title_sort korrigan1 interacts specifically with integral components of the cellulose synthase machinery
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4226561/
https://www.ncbi.nlm.nih.gov/pubmed/25383767
http://dx.doi.org/10.1371/journal.pone.0112387
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