Protein S-nitrosylation under abiotic stress: Role and mechanism

Abiotic stress is one of the main threats affecting crop growth and production. Nitric oxide (NO), an important signaling molecule involved in wide range of plant growth and development as well as in response to abiotic stress. NO can exert its biological functions through protein S-nitrosylation, a...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry 2024-02, Vol.207, p.108329-108329, Article 108329
Hauptverfasser: Wang, Tong, Hou, Xuemei, Wei, Lijuan, Deng, Yuzheng, Zhao, Zongxi, Liang, Chen, Liao, Weibiao
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 108329
container_issue
container_start_page 108329
container_title Plant physiology and biochemistry
container_volume 207
creator Wang, Tong
Hou, Xuemei
Wei, Lijuan
Deng, Yuzheng
Zhao, Zongxi
Liang, Chen
Liao, Weibiao
description Abiotic stress is one of the main threats affecting crop growth and production. Nitric oxide (NO), an important signaling molecule involved in wide range of plant growth and development as well as in response to abiotic stress. NO can exert its biological functions through protein S-nitrosylation, a redox-based posttranslational modification by covalently adding NO moiety to a reactive cysteine thiol of a target protein to form an S-nitrosothiol (SNO). Protein S-nitrosylation is an evolutionarily conserved mechanism regulating multiple aspects of cellular signaling in plant. Recently, emerging evidence have elucidated protein S-nitrosylation as a modulator of plant in responses to abiotic stress, including salt stress, extreme temperature stress, light stress, heavy metal and drought stress. In addition, significant mechanism has been made in functional characterization of protein S-nitrosylated candidates, such as changing protein conformation, and the subcellular localization of proteins, regulating protein activity and influencing protein interactions. In this study, we updated the data related to protein S-nitrosylation in plants in response to adversity and gained a deeper understanding of the functional changes of target proteins after protein S-nitrosylation. •Protein S-nitrosylation plays a critical role in plant response to abiotic stress.•Protein S-nitrosylation regulates enzyme activity under abiotic stress.•S-nitrosylation affect protein function under abiotic stress.•S-nitrosylation changes protein subcellular localization and interactions under stress.
doi_str_mv 10.1016/j.plaphy.2023.108329
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_3153625337</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0981942823008409</els_id><sourcerecordid>2911844144</sourcerecordid><originalsourceid>FETCH-LOGICAL-c344t-16e9af2ce82f3881045d17613a1c86b829820a43db020db8fd9f916ac798eb973</originalsourceid><addsrcrecordid>eNqFkMtKxDAUhoMozjj6BiJduumY27SJC1EGbzCgeFmHNDllMrRpTVph3t4OVZe6OnD4_vNzPoROCZ4TTLKLzbytdLvezimmbFgJRuUemhKRs5RmEu-jKZaCpJJTMUFHMW4wxpTn7BBNmCCCC8Gm6Po5NB04n7ym3nWhidtKd67xSe8thEQXrumcSWIXIMbL5KWpINHeJjWYtfYu1sfooNRVhJPvOUPvd7dvy4d09XT_uLxZpYZx3qUkA6lLakDQkglBMF9YkmeEaWJEVggqBcWaM1tgim0hSitLSTJtcimgkDmbofPxbhuajx5ip2oXDVSV9tD0UTGyYBldMPY_SiUZ3ueE8wHlI2qG12OAUrXB1TpsFcFqp1lt1KhZ7TSrUfMQO_tu6Isa7G_ox-sAXI0ADEo-HQQVjQNvwLoAplO2cX83fAGvt47K</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2911844144</pqid></control><display><type>article</type><title>Protein S-nitrosylation under abiotic stress: Role and mechanism</title><source>Elsevier ScienceDirect Journals</source><creator>Wang, Tong ; Hou, Xuemei ; Wei, Lijuan ; Deng, Yuzheng ; Zhao, Zongxi ; Liang, Chen ; Liao, Weibiao</creator><creatorcontrib>Wang, Tong ; Hou, Xuemei ; Wei, Lijuan ; Deng, Yuzheng ; Zhao, Zongxi ; Liang, Chen ; Liao, Weibiao</creatorcontrib><description>Abiotic stress is one of the main threats affecting crop growth and production. Nitric oxide (NO), an important signaling molecule involved in wide range of plant growth and development as well as in response to abiotic stress. NO can exert its biological functions through protein S-nitrosylation, a redox-based posttranslational modification by covalently adding NO moiety to a reactive cysteine thiol of a target protein to form an S-nitrosothiol (SNO). Protein S-nitrosylation is an evolutionarily conserved mechanism regulating multiple aspects of cellular signaling in plant. Recently, emerging evidence have elucidated protein S-nitrosylation as a modulator of plant in responses to abiotic stress, including salt stress, extreme temperature stress, light stress, heavy metal and drought stress. In addition, significant mechanism has been made in functional characterization of protein S-nitrosylated candidates, such as changing protein conformation, and the subcellular localization of proteins, regulating protein activity and influencing protein interactions. In this study, we updated the data related to protein S-nitrosylation in plants in response to adversity and gained a deeper understanding of the functional changes of target proteins after protein S-nitrosylation. •Protein S-nitrosylation plays a critical role in plant response to abiotic stress.•Protein S-nitrosylation regulates enzyme activity under abiotic stress.•S-nitrosylation affect protein function under abiotic stress.•S-nitrosylation changes protein subcellular localization and interactions under stress.</description><identifier>ISSN: 0981-9428</identifier><identifier>EISSN: 1873-2690</identifier><identifier>DOI: 10.1016/j.plaphy.2023.108329</identifier><identifier>PMID: 38184883</identifier><language>eng</language><publisher>France: Elsevier Masson SAS</publisher><subject>Abiotic stress ; chemical bonding ; cysteine ; growth and development ; heavy metals ; moieties ; Nitric oxide ; plant growth ; post-translational modification ; protein conformation ; S-nitrosoglutathione reductase ; S-nitrosylation ; salt stress ; Sub-cellular localization ; temperature ; thiols ; water stress</subject><ispartof>Plant physiology and biochemistry, 2024-02, Vol.207, p.108329-108329, Article 108329</ispartof><rights>2024 Elsevier Masson SAS</rights><rights>Copyright © 2024 Elsevier Masson SAS. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c344t-16e9af2ce82f3881045d17613a1c86b829820a43db020db8fd9f916ac798eb973</cites><orcidid>0000-0002-7404-2145</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0981942823008409$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38184883$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Tong</creatorcontrib><creatorcontrib>Hou, Xuemei</creatorcontrib><creatorcontrib>Wei, Lijuan</creatorcontrib><creatorcontrib>Deng, Yuzheng</creatorcontrib><creatorcontrib>Zhao, Zongxi</creatorcontrib><creatorcontrib>Liang, Chen</creatorcontrib><creatorcontrib>Liao, Weibiao</creatorcontrib><title>Protein S-nitrosylation under abiotic stress: Role and mechanism</title><title>Plant physiology and biochemistry</title><addtitle>Plant Physiol Biochem</addtitle><description>Abiotic stress is one of the main threats affecting crop growth and production. Nitric oxide (NO), an important signaling molecule involved in wide range of plant growth and development as well as in response to abiotic stress. NO can exert its biological functions through protein S-nitrosylation, a redox-based posttranslational modification by covalently adding NO moiety to a reactive cysteine thiol of a target protein to form an S-nitrosothiol (SNO). Protein S-nitrosylation is an evolutionarily conserved mechanism regulating multiple aspects of cellular signaling in plant. Recently, emerging evidence have elucidated protein S-nitrosylation as a modulator of plant in responses to abiotic stress, including salt stress, extreme temperature stress, light stress, heavy metal and drought stress. In addition, significant mechanism has been made in functional characterization of protein S-nitrosylated candidates, such as changing protein conformation, and the subcellular localization of proteins, regulating protein activity and influencing protein interactions. In this study, we updated the data related to protein S-nitrosylation in plants in response to adversity and gained a deeper understanding of the functional changes of target proteins after protein S-nitrosylation. •Protein S-nitrosylation plays a critical role in plant response to abiotic stress.•Protein S-nitrosylation regulates enzyme activity under abiotic stress.•S-nitrosylation affect protein function under abiotic stress.•S-nitrosylation changes protein subcellular localization and interactions under stress.</description><subject>Abiotic stress</subject><subject>chemical bonding</subject><subject>cysteine</subject><subject>growth and development</subject><subject>heavy metals</subject><subject>moieties</subject><subject>Nitric oxide</subject><subject>plant growth</subject><subject>post-translational modification</subject><subject>protein conformation</subject><subject>S-nitrosoglutathione reductase</subject><subject>S-nitrosylation</subject><subject>salt stress</subject><subject>Sub-cellular localization</subject><subject>temperature</subject><subject>thiols</subject><subject>water stress</subject><issn>0981-9428</issn><issn>1873-2690</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><recordid>eNqFkMtKxDAUhoMozjj6BiJduumY27SJC1EGbzCgeFmHNDllMrRpTVph3t4OVZe6OnD4_vNzPoROCZ4TTLKLzbytdLvezimmbFgJRuUemhKRs5RmEu-jKZaCpJJTMUFHMW4wxpTn7BBNmCCCC8Gm6Po5NB04n7ym3nWhidtKd67xSe8thEQXrumcSWIXIMbL5KWpINHeJjWYtfYu1sfooNRVhJPvOUPvd7dvy4d09XT_uLxZpYZx3qUkA6lLakDQkglBMF9YkmeEaWJEVggqBcWaM1tgim0hSitLSTJtcimgkDmbofPxbhuajx5ip2oXDVSV9tD0UTGyYBldMPY_SiUZ3ueE8wHlI2qG12OAUrXB1TpsFcFqp1lt1KhZ7TSrUfMQO_tu6Isa7G_ox-sAXI0ADEo-HQQVjQNvwLoAplO2cX83fAGvt47K</recordid><startdate>20240201</startdate><enddate>20240201</enddate><creator>Wang, Tong</creator><creator>Hou, Xuemei</creator><creator>Wei, Lijuan</creator><creator>Deng, Yuzheng</creator><creator>Zhao, Zongxi</creator><creator>Liang, Chen</creator><creator>Liao, Weibiao</creator><general>Elsevier Masson SAS</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><orcidid>https://orcid.org/0000-0002-7404-2145</orcidid></search><sort><creationdate>20240201</creationdate><title>Protein S-nitrosylation under abiotic stress: Role and mechanism</title><author>Wang, Tong ; Hou, Xuemei ; Wei, Lijuan ; Deng, Yuzheng ; Zhao, Zongxi ; Liang, Chen ; Liao, Weibiao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c344t-16e9af2ce82f3881045d17613a1c86b829820a43db020db8fd9f916ac798eb973</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Abiotic stress</topic><topic>chemical bonding</topic><topic>cysteine</topic><topic>growth and development</topic><topic>heavy metals</topic><topic>moieties</topic><topic>Nitric oxide</topic><topic>plant growth</topic><topic>post-translational modification</topic><topic>protein conformation</topic><topic>S-nitrosoglutathione reductase</topic><topic>S-nitrosylation</topic><topic>salt stress</topic><topic>Sub-cellular localization</topic><topic>temperature</topic><topic>thiols</topic><topic>water stress</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Tong</creatorcontrib><creatorcontrib>Hou, Xuemei</creatorcontrib><creatorcontrib>Wei, Lijuan</creatorcontrib><creatorcontrib>Deng, Yuzheng</creatorcontrib><creatorcontrib>Zhao, Zongxi</creatorcontrib><creatorcontrib>Liang, Chen</creatorcontrib><creatorcontrib>Liao, Weibiao</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>Plant physiology and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Tong</au><au>Hou, Xuemei</au><au>Wei, Lijuan</au><au>Deng, Yuzheng</au><au>Zhao, Zongxi</au><au>Liang, Chen</au><au>Liao, Weibiao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein S-nitrosylation under abiotic stress: Role and mechanism</atitle><jtitle>Plant physiology and biochemistry</jtitle><addtitle>Plant Physiol Biochem</addtitle><date>2024-02-01</date><risdate>2024</risdate><volume>207</volume><spage>108329</spage><epage>108329</epage><pages>108329-108329</pages><artnum>108329</artnum><issn>0981-9428</issn><eissn>1873-2690</eissn><abstract>Abiotic stress is one of the main threats affecting crop growth and production. Nitric oxide (NO), an important signaling molecule involved in wide range of plant growth and development as well as in response to abiotic stress. NO can exert its biological functions through protein S-nitrosylation, a redox-based posttranslational modification by covalently adding NO moiety to a reactive cysteine thiol of a target protein to form an S-nitrosothiol (SNO). Protein S-nitrosylation is an evolutionarily conserved mechanism regulating multiple aspects of cellular signaling in plant. Recently, emerging evidence have elucidated protein S-nitrosylation as a modulator of plant in responses to abiotic stress, including salt stress, extreme temperature stress, light stress, heavy metal and drought stress. In addition, significant mechanism has been made in functional characterization of protein S-nitrosylated candidates, such as changing protein conformation, and the subcellular localization of proteins, regulating protein activity and influencing protein interactions. In this study, we updated the data related to protein S-nitrosylation in plants in response to adversity and gained a deeper understanding of the functional changes of target proteins after protein S-nitrosylation. •Protein S-nitrosylation plays a critical role in plant response to abiotic stress.•Protein S-nitrosylation regulates enzyme activity under abiotic stress.•S-nitrosylation affect protein function under abiotic stress.•S-nitrosylation changes protein subcellular localization and interactions under stress.</abstract><cop>France</cop><pub>Elsevier Masson SAS</pub><pmid>38184883</pmid><doi>10.1016/j.plaphy.2023.108329</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-7404-2145</orcidid></addata></record>
fulltext fulltext
identifier ISSN: 0981-9428
ispartof Plant physiology and biochemistry, 2024-02, Vol.207, p.108329-108329, Article 108329
issn 0981-9428
1873-2690
language eng
recordid cdi_proquest_miscellaneous_3153625337
source Elsevier ScienceDirect Journals
subjects Abiotic stress
chemical bonding
cysteine
growth and development
heavy metals
moieties
Nitric oxide
plant growth
post-translational modification
protein conformation
S-nitrosoglutathione reductase
S-nitrosylation
salt stress
Sub-cellular localization
temperature
thiols
water stress
title Protein S-nitrosylation under abiotic stress: Role and mechanism
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-01T13%3A56%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Protein%20S-nitrosylation%20under%20abiotic%20stress:%20Role%20and%20mechanism&rft.jtitle=Plant%20physiology%20and%20biochemistry&rft.au=Wang,%20Tong&rft.date=2024-02-01&rft.volume=207&rft.spage=108329&rft.epage=108329&rft.pages=108329-108329&rft.artnum=108329&rft.issn=0981-9428&rft.eissn=1873-2690&rft_id=info:doi/10.1016/j.plaphy.2023.108329&rft_dat=%3Cproquest_cross%3E2911844144%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2911844144&rft_id=info:pmid/38184883&rft_els_id=S0981942823008409&rfr_iscdi=true