Current Understanding of Temperature Stress-Responsive Chloroplast FtsH Metalloproteases

Low and high temperatures are life-threatening stress factors, diminishing plant productivity. One of the earliest responses of plants to stress is a rapid burst of reactive oxygen species (ROS) in chloroplasts. Widespread efforts over the past decade shed new light on the chloroplast as an environm...

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Autores principales:	Shengji Luo, Chanhong Kim
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	FILAMENTOUS TEMPERATURE-SENSITIVE H protein quality control proteostasis retrograde signaling reactive oxygen species Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/25a6e935a1e54c8397bcf5dcbc9cbe47
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spelling	oai:doaj.org-article:25a6e935a1e54c8397bcf5dcbc9cbe472021-11-25T17:53:28ZCurrent Understanding of Temperature Stress-Responsive Chloroplast FtsH Metalloproteases10.3390/ijms2222121061422-00671661-6596https://doaj.org/article/25a6e935a1e54c8397bcf5dcbc9cbe472021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/22/12106https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Low and high temperatures are life-threatening stress factors, diminishing plant productivity. One of the earliest responses of plants to stress is a rapid burst of reactive oxygen species (ROS) in chloroplasts. Widespread efforts over the past decade shed new light on the chloroplast as an environmental sensor, translating the environmental fluctuation into varying physiological responses by utilizing distinct retrograde (chloroplast-to-nucleus) signals. Recent studies have unveiled that chloroplasts mediate a similar unfolded/misfolded/damaged protein response (cpUPR) as observed in the endoplasmic reticulum and mitochondria. Although observing cpUPR is not surprising since the chloroplast is a prime organelle producing harmful ROS, the intertwined relationship among ROS, protein damage, and chloroplast protein quality controls (cpPQCs) with retrograde signaling has recently been reported. This finding also gives rise to critical attention on chloroplast proteins involved in cpPQCs, ROS detoxifiers, transcription/translation, import of precursor proteins, and assembly/maturation, the deficiency of which compromises chloroplast protein homeostasis (proteostasis). Any perturbation in the protein may require readjustment of proteostasis by transmitting retrograde signal(s) to the nucleus, whose genome encodes most of the chloroplast proteins involved in proteostasis. This review focuses on recent findings on cpUPR and chloroplast-targeted FILAMENTOUS TEMPERATURE-SENSITIVE H proteases involved in cpPQC and retrograde signaling and their impacts on plant responses to temperature stress.Shengji LuoChanhong KimMDPI AGarticleFILAMENTOUS TEMPERATURE-SENSITIVE Hprotein quality controlproteostasisretrograde signalingreactive oxygen speciesBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 12106, p 12106 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	FILAMENTOUS TEMPERATURE-SENSITIVE H protein quality control proteostasis retrograde signaling reactive oxygen species Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	FILAMENTOUS TEMPERATURE-SENSITIVE H protein quality control proteostasis retrograde signaling reactive oxygen species Biology (General) QH301-705.5 Chemistry QD1-999 Shengji Luo Chanhong Kim Current Understanding of Temperature Stress-Responsive Chloroplast FtsH Metalloproteases
description	Low and high temperatures are life-threatening stress factors, diminishing plant productivity. One of the earliest responses of plants to stress is a rapid burst of reactive oxygen species (ROS) in chloroplasts. Widespread efforts over the past decade shed new light on the chloroplast as an environmental sensor, translating the environmental fluctuation into varying physiological responses by utilizing distinct retrograde (chloroplast-to-nucleus) signals. Recent studies have unveiled that chloroplasts mediate a similar unfolded/misfolded/damaged protein response (cpUPR) as observed in the endoplasmic reticulum and mitochondria. Although observing cpUPR is not surprising since the chloroplast is a prime organelle producing harmful ROS, the intertwined relationship among ROS, protein damage, and chloroplast protein quality controls (cpPQCs) with retrograde signaling has recently been reported. This finding also gives rise to critical attention on chloroplast proteins involved in cpPQCs, ROS detoxifiers, transcription/translation, import of precursor proteins, and assembly/maturation, the deficiency of which compromises chloroplast protein homeostasis (proteostasis). Any perturbation in the protein may require readjustment of proteostasis by transmitting retrograde signal(s) to the nucleus, whose genome encodes most of the chloroplast proteins involved in proteostasis. This review focuses on recent findings on cpUPR and chloroplast-targeted FILAMENTOUS TEMPERATURE-SENSITIVE H proteases involved in cpPQC and retrograde signaling and their impacts on plant responses to temperature stress.
format	article
author	Shengji Luo Chanhong Kim
author_facet	Shengji Luo Chanhong Kim
author_sort	Shengji Luo
title	Current Understanding of Temperature Stress-Responsive Chloroplast FtsH Metalloproteases
title_short	Current Understanding of Temperature Stress-Responsive Chloroplast FtsH Metalloproteases
title_full	Current Understanding of Temperature Stress-Responsive Chloroplast FtsH Metalloproteases
title_fullStr	Current Understanding of Temperature Stress-Responsive Chloroplast FtsH Metalloproteases
title_full_unstemmed	Current Understanding of Temperature Stress-Responsive Chloroplast FtsH Metalloproteases
title_sort	current understanding of temperature stress-responsive chloroplast ftsh metalloproteases
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/25a6e935a1e54c8397bcf5dcbc9cbe47
work_keys_str_mv	AT shengjiluo currentunderstandingoftemperaturestressresponsivechloroplastftshmetalloproteases AT chanhongkim currentunderstandingoftemperaturestressresponsivechloroplastftshmetalloproteases
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Current Understanding of Temperature Stress-Responsive Chloroplast FtsH Metalloproteases

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