Lon domain-containing protein 1 represses thioredoxin y2 and regulates ROS levels in Arabidopsis chloroplasts

Jin Seok Shin; Soo Youn Kim; Won Mi So; Minsoo Noh; Kyoung Shin Yoo; Jeong Sheop Shin

doi:10.1002/1873-3468.13664

Lon domain-containing protein 1 represses thioredoxin y2 and regulates ROS levels in Arabidopsis chloroplasts

Jin Seok Shin, Soo Youn Kim, Won Mi So, Minsoo Noh, Kyoung Shin Yoo, Jeong Sheop Shin

Division of life Sciences

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

Plant thioredoxins (Trxs) act as antioxidants and function as redox regulators in the chloroplast. Although the regulation of ROS in chloroplasts is well elucidated, the precise regulation mechanism of Trx remains unknown. Here, we characterize a novel chloroplast protein, Lon domain-containing protein 1 (LCP1), which contains only a Lon domain, the precise function of which is not known. We find that LCP1 interacts with Trx-y2 and represses its activity, and that knockdown (KD) of LCP1 causes anther indehiscence due to deficient lignin deposition. In addition, LCP1 KD plants show less ROS accumulation and lower expression of ROS-responsive marker genes than the wild-type plant. Taken together, we suggest that LCP1 directly regulates Trx-y2 and controls H₂O₂ levels and, thereby, regulates lignin polymerization in the anther endothecium.

Original language	English
Pages (from-to)	986-994
Number of pages	9
Journal	FEBS Letters
Volume	594
Issue number	6
DOIs	https://doi.org/10.1002/1873-3468.13664
Publication status	Published - 2020 Mar 1

Bibliographical note

Funding Information:
This work was supported by two grants (2014R1A2A2A01005974 and 2019R1F1A1060014) from the National Research Foundation of Korea (NRF) funded by the Ministry of Science and by a grant PJ01367001 from the Next‐Generation BioGreen 21 Program funded by the Rural Development Administration, Republic of Korea. This work was also partially supported by Korea University.

Funding Information:
This work was supported by two grants (2014R1A2A2A01005974 and 2019R1F1A1060014) from the National Research Foundation of Korea (NRF) funded by the Ministry of Science and by a grant PJ01367001 from the Next-Generation BioGreen 21 Program funded by the Rural Development Administration, Republic of Korea. This work was also partially supported by Korea University.

Publisher Copyright:
© 2019 Federation of European Biochemical Societies

Keywords

Arabidopsis
ROS
chloroplast
dehiscence
lignification
thioredoxin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1002/1873-3468.13664

Cite this

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title = "Lon domain-containing protein 1 represses thioredoxin y2 and regulates ROS levels in Arabidopsis chloroplasts",

abstract = "Plant thioredoxins (Trxs) act as antioxidants and function as redox regulators in the chloroplast. Although the regulation of ROS in chloroplasts is well elucidated, the precise regulation mechanism of Trx remains unknown. Here, we characterize a novel chloroplast protein, Lon domain-containing protein 1 (LCP1), which contains only a Lon domain, the precise function of which is not known. We find that LCP1 interacts with Trx-y2 and represses its activity, and that knockdown (KD) of LCP1 causes anther indehiscence due to deficient lignin deposition. In addition, LCP1 KD plants show less ROS accumulation and lower expression of ROS-responsive marker genes than the wild-type plant. Taken together, we suggest that LCP1 directly regulates Trx-y2 and controls H2O2 levels and, thereby, regulates lignin polymerization in the anther endothecium.",

keywords = "Arabidopsis, ROS, chloroplast, dehiscence, lignification, thioredoxin",

author = "Shin, {Jin Seok} and Kim, {Soo Youn} and So, {Won Mi} and Minsoo Noh and Yoo, {Kyoung Shin} and Shin, {Jeong Sheop}",

note = "Funding Information: This work was supported by two grants (2014R1A2A2A01005974 and 2019R1F1A1060014) from the National Research Foundation of Korea (NRF) funded by the Ministry of Science and by a grant PJ01367001 from the Next‐Generation BioGreen 21 Program funded by the Rural Development Administration, Republic of Korea. This work was also partially supported by Korea University. Funding Information: This work was supported by two grants (2014R1A2A2A01005974 and 2019R1F1A1060014) from the National Research Foundation of Korea (NRF) funded by the Ministry of Science and by a grant PJ01367001 from the Next-Generation BioGreen 21 Program funded by the Rural Development Administration, Republic of Korea. This work was also partially supported by Korea University. Publisher Copyright: {\textcopyright} 2019 Federation of European Biochemical Societies",

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T1 - Lon domain-containing protein 1 represses thioredoxin y2 and regulates ROS levels in Arabidopsis chloroplasts

AU - Shin, Jin Seok

AU - Kim, Soo Youn

AU - So, Won Mi

AU - Noh, Minsoo

AU - Yoo, Kyoung Shin

AU - Shin, Jeong Sheop

N1 - Funding Information: This work was supported by two grants (2014R1A2A2A01005974 and 2019R1F1A1060014) from the National Research Foundation of Korea (NRF) funded by the Ministry of Science and by a grant PJ01367001 from the Next‐Generation BioGreen 21 Program funded by the Rural Development Administration, Republic of Korea. This work was also partially supported by Korea University. Funding Information: This work was supported by two grants (2014R1A2A2A01005974 and 2019R1F1A1060014) from the National Research Foundation of Korea (NRF) funded by the Ministry of Science and by a grant PJ01367001 from the Next-Generation BioGreen 21 Program funded by the Rural Development Administration, Republic of Korea. This work was also partially supported by Korea University. Publisher Copyright: © 2019 Federation of European Biochemical Societies

PY - 2020/3/1

Y1 - 2020/3/1

N2 - Plant thioredoxins (Trxs) act as antioxidants and function as redox regulators in the chloroplast. Although the regulation of ROS in chloroplasts is well elucidated, the precise regulation mechanism of Trx remains unknown. Here, we characterize a novel chloroplast protein, Lon domain-containing protein 1 (LCP1), which contains only a Lon domain, the precise function of which is not known. We find that LCP1 interacts with Trx-y2 and represses its activity, and that knockdown (KD) of LCP1 causes anther indehiscence due to deficient lignin deposition. In addition, LCP1 KD plants show less ROS accumulation and lower expression of ROS-responsive marker genes than the wild-type plant. Taken together, we suggest that LCP1 directly regulates Trx-y2 and controls H2O2 levels and, thereby, regulates lignin polymerization in the anther endothecium.

AB - Plant thioredoxins (Trxs) act as antioxidants and function as redox regulators in the chloroplast. Although the regulation of ROS in chloroplasts is well elucidated, the precise regulation mechanism of Trx remains unknown. Here, we characterize a novel chloroplast protein, Lon domain-containing protein 1 (LCP1), which contains only a Lon domain, the precise function of which is not known. We find that LCP1 interacts with Trx-y2 and represses its activity, and that knockdown (KD) of LCP1 causes anther indehiscence due to deficient lignin deposition. In addition, LCP1 KD plants show less ROS accumulation and lower expression of ROS-responsive marker genes than the wild-type plant. Taken together, we suggest that LCP1 directly regulates Trx-y2 and controls H2O2 levels and, thereby, regulates lignin polymerization in the anther endothecium.

KW - Arabidopsis

KW - ROS

KW - chloroplast

KW - dehiscence

KW - lignification

KW - thioredoxin

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JF - FEBS Letters

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ER -

Lon domain-containing protein 1 represses thioredoxin y2 and regulates ROS levels in Arabidopsis chloroplasts

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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