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Proteomic analysis of haem-binding protein from Arabidopsis thaliana and Cyanidioschyzon merolae

Chloroplast biogenesis involves the coordinated expression of the plastid and nuclear genomes, requiring information to be sent from the nucleus to the developing chloroplasts and vice versa. Although it is well known how the nucleus controls chloroplast development, it is still poorly understood ho...

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Autores principales: Shimizu, Takayuki, Yasuda, Rintaro, Mukai, Yui, Tanoue, Ryo, Shimada, Tomohiro, Imamura, Sousuke, Tanaka, Kan, Watanabe, Satoru, Masuda, Tatsuru
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7209954/
https://www.ncbi.nlm.nih.gov/pubmed/32362261
http://dx.doi.org/10.1098/rstb.2019.0488
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author Shimizu, Takayuki
Yasuda, Rintaro
Mukai, Yui
Tanoue, Ryo
Shimada, Tomohiro
Imamura, Sousuke
Tanaka, Kan
Watanabe, Satoru
Masuda, Tatsuru
author_facet Shimizu, Takayuki
Yasuda, Rintaro
Mukai, Yui
Tanoue, Ryo
Shimada, Tomohiro
Imamura, Sousuke
Tanaka, Kan
Watanabe, Satoru
Masuda, Tatsuru
author_sort Shimizu, Takayuki
collection PubMed
description Chloroplast biogenesis involves the coordinated expression of the plastid and nuclear genomes, requiring information to be sent from the nucleus to the developing chloroplasts and vice versa. Although it is well known how the nucleus controls chloroplast development, it is still poorly understood how the plastid communicates with the nucleus. Currently, haem is proposed as a plastid-to-nucleus (retrograde) signal that is involved in various physiological regulations, such as photosynthesis-associated nuclear genes expression and cell cycle in plants and algae. However, components that transduce haem-dependent signalling are still unidentified. In this study, by using haem-immobilized high-performance affinity beads, we performed proteomic analysis of haem-binding proteins from Arabidopsis thaliana and Cyanidioschyzon merolae. Most of the identified proteins were non-canonical haemoproteins localized in various organelles. Interestingly, half of the identified proteins were nucleus proteins, some of them have a similar function or localization in either or both organisms. Following biochemical analysis of selective proteins demonstrated haem binding. This study firstly demonstrates that nucleus proteins in plant and algae show haem-binding properties. This article is part of the theme issue ‘Retrograde signalling from endosymbiotic organelles’.
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spelling pubmed-72099542020-05-18 Proteomic analysis of haem-binding protein from Arabidopsis thaliana and Cyanidioschyzon merolae Shimizu, Takayuki Yasuda, Rintaro Mukai, Yui Tanoue, Ryo Shimada, Tomohiro Imamura, Sousuke Tanaka, Kan Watanabe, Satoru Masuda, Tatsuru Philos Trans R Soc Lond B Biol Sci Articles Chloroplast biogenesis involves the coordinated expression of the plastid and nuclear genomes, requiring information to be sent from the nucleus to the developing chloroplasts and vice versa. Although it is well known how the nucleus controls chloroplast development, it is still poorly understood how the plastid communicates with the nucleus. Currently, haem is proposed as a plastid-to-nucleus (retrograde) signal that is involved in various physiological regulations, such as photosynthesis-associated nuclear genes expression and cell cycle in plants and algae. However, components that transduce haem-dependent signalling are still unidentified. In this study, by using haem-immobilized high-performance affinity beads, we performed proteomic analysis of haem-binding proteins from Arabidopsis thaliana and Cyanidioschyzon merolae. Most of the identified proteins were non-canonical haemoproteins localized in various organelles. Interestingly, half of the identified proteins were nucleus proteins, some of them have a similar function or localization in either or both organisms. Following biochemical analysis of selective proteins demonstrated haem binding. This study firstly demonstrates that nucleus proteins in plant and algae show haem-binding properties. This article is part of the theme issue ‘Retrograde signalling from endosymbiotic organelles’. The Royal Society 2020-06-22 2020-05-04 /pmc/articles/PMC7209954/ /pubmed/32362261 http://dx.doi.org/10.1098/rstb.2019.0488 Text en © 2020 The Authors. http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/http://creativecommons.org/licenses/by/4.0/Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.
spellingShingle Articles
Shimizu, Takayuki
Yasuda, Rintaro
Mukai, Yui
Tanoue, Ryo
Shimada, Tomohiro
Imamura, Sousuke
Tanaka, Kan
Watanabe, Satoru
Masuda, Tatsuru
Proteomic analysis of haem-binding protein from Arabidopsis thaliana and Cyanidioschyzon merolae
title Proteomic analysis of haem-binding protein from Arabidopsis thaliana and Cyanidioschyzon merolae
title_full Proteomic analysis of haem-binding protein from Arabidopsis thaliana and Cyanidioschyzon merolae
title_fullStr Proteomic analysis of haem-binding protein from Arabidopsis thaliana and Cyanidioschyzon merolae
title_full_unstemmed Proteomic analysis of haem-binding protein from Arabidopsis thaliana and Cyanidioschyzon merolae
title_short Proteomic analysis of haem-binding protein from Arabidopsis thaliana and Cyanidioschyzon merolae
title_sort proteomic analysis of haem-binding protein from arabidopsis thaliana and cyanidioschyzon merolae
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7209954/
https://www.ncbi.nlm.nih.gov/pubmed/32362261
http://dx.doi.org/10.1098/rstb.2019.0488
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