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Disrupting the bimolecular binding of the haem-binding protein 5 (AtHBP5) to haem oxygenase 1 (HY1) leads to oxidative stress in Arabidopsis
The Arabidopsis thaliana L. SOUL/haem-binding proteins, AtHBPs belong to a family of five members. The Arabidopsis cytosolic AtHBP1 (At1g17100) and AtHBP2 (At2g37970) have been shown to bind porphyrins and metalloporphyrins including haem. In contrast to the cytosolic localization of these haem-bind...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3467301/ https://www.ncbi.nlm.nih.gov/pubmed/22991161 http://dx.doi.org/10.1093/jxb/ers242 |
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author | Lee, Hye-Jung Mochizuki, Nobuyoshi Masuda, Tatsuru Buckhout, Thomas J. |
author_facet | Lee, Hye-Jung Mochizuki, Nobuyoshi Masuda, Tatsuru Buckhout, Thomas J. |
author_sort | Lee, Hye-Jung |
collection | PubMed |
description | The Arabidopsis thaliana L. SOUL/haem-binding proteins, AtHBPs belong to a family of five members. The Arabidopsis cytosolic AtHBP1 (At1g17100) and AtHBP2 (At2g37970) have been shown to bind porphyrins and metalloporphyrins including haem. In contrast to the cytosolic localization of these haem-binding proteins, AtHBP5 (At5g20140) encodes a protein with an N-terminal transit peptide that probably directs targeting to the chloroplast. In this report, it is shown that AtHBP5 binds haem and interacts with the haem oxygenase, HY1, in both yeast two-hybrid and BiFC assays. The expression of HY1 is repressed in the athbp5 T-DNA knockdown mutant and the accumulation of H(2)O(2) is observed in athbp5 seedlings that are treated with methyl jasmonate (MeJA), a ROS-producing stress hormone. In contrast, AtHBP5 over-expressing plants show a decreased accumulation of H(2)O(2) after MeJA treatment compared with the controls. It is proposed that the interaction between the HY1 and AtHBP5 proteins participate in an antioxidant pathway that might be mediated by reaction products of haem catabolism. |
format | Online Article Text |
id | pubmed-3467301 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-34673012012-10-10 Disrupting the bimolecular binding of the haem-binding protein 5 (AtHBP5) to haem oxygenase 1 (HY1) leads to oxidative stress in Arabidopsis Lee, Hye-Jung Mochizuki, Nobuyoshi Masuda, Tatsuru Buckhout, Thomas J. J Exp Bot Research Paper The Arabidopsis thaliana L. SOUL/haem-binding proteins, AtHBPs belong to a family of five members. The Arabidopsis cytosolic AtHBP1 (At1g17100) and AtHBP2 (At2g37970) have been shown to bind porphyrins and metalloporphyrins including haem. In contrast to the cytosolic localization of these haem-binding proteins, AtHBP5 (At5g20140) encodes a protein with an N-terminal transit peptide that probably directs targeting to the chloroplast. In this report, it is shown that AtHBP5 binds haem and interacts with the haem oxygenase, HY1, in both yeast two-hybrid and BiFC assays. The expression of HY1 is repressed in the athbp5 T-DNA knockdown mutant and the accumulation of H(2)O(2) is observed in athbp5 seedlings that are treated with methyl jasmonate (MeJA), a ROS-producing stress hormone. In contrast, AtHBP5 over-expressing plants show a decreased accumulation of H(2)O(2) after MeJA treatment compared with the controls. It is proposed that the interaction between the HY1 and AtHBP5 proteins participate in an antioxidant pathway that might be mediated by reaction products of haem catabolism. Oxford University Press 2012-10 2012-09-24 /pmc/articles/PMC3467301/ /pubmed/22991161 http://dx.doi.org/10.1093/jxb/ers242 Text en © 2012 The Authors. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Lee, Hye-Jung Mochizuki, Nobuyoshi Masuda, Tatsuru Buckhout, Thomas J. Disrupting the bimolecular binding of the haem-binding protein 5 (AtHBP5) to haem oxygenase 1 (HY1) leads to oxidative stress in Arabidopsis |
title | Disrupting the bimolecular binding of the haem-binding protein 5 (AtHBP5) to
haem oxygenase 1 (HY1) leads to oxidative stress in Arabidopsis
|
title_full | Disrupting the bimolecular binding of the haem-binding protein 5 (AtHBP5) to
haem oxygenase 1 (HY1) leads to oxidative stress in Arabidopsis
|
title_fullStr | Disrupting the bimolecular binding of the haem-binding protein 5 (AtHBP5) to
haem oxygenase 1 (HY1) leads to oxidative stress in Arabidopsis
|
title_full_unstemmed | Disrupting the bimolecular binding of the haem-binding protein 5 (AtHBP5) to
haem oxygenase 1 (HY1) leads to oxidative stress in Arabidopsis
|
title_short | Disrupting the bimolecular binding of the haem-binding protein 5 (AtHBP5) to
haem oxygenase 1 (HY1) leads to oxidative stress in Arabidopsis
|
title_sort | disrupting the bimolecular binding of the haem-binding protein 5 (athbp5) to
haem oxygenase 1 (hy1) leads to oxidative stress in arabidopsis |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3467301/ https://www.ncbi.nlm.nih.gov/pubmed/22991161 http://dx.doi.org/10.1093/jxb/ers242 |
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