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Protein S-nitrosation differentially modulates tomato responses to infection by hemi-biotrophic oomycetes of Phytophthora spp
Regulation of protein function by reversible S-nitrosation, a post-translational modification based on the attachment of nitroso group to cysteine thiols, has emerged among key mechanisms of NO signalling in plant development and stress responses. S-nitrosoglutathione is regarded as the most abundan...
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Published in: | Horticulture research 2021-02, Vol.8 (1), Article 34 |
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description | Regulation of protein function by reversible S-nitrosation, a post-translational modification based on the attachment of nitroso group to cysteine thiols, has emerged among key mechanisms of NO signalling in plant development and stress responses. S-nitrosoglutathione is regarded as the most abundant low-molecular-weight S-nitrosothiol in plants, where its intracellular concentrations are modulated by S-nitrosoglutathione reductase. We analysed modulations of S-nitrosothiols and protein S-nitrosation mediated by S-nitrosoglutathione reductase in cultivated
Solanum lycopersicum
(susceptible) and wild
Solanum habrochaites
(resistant genotype) up to 96 h post inoculation (hpi) by two hemibiotrophic oomycetes,
Phytophthora infestans
and
Phytophthora parasitica
. S-nitrosoglutathione reductase activity and protein level were decreased by
P. infestans
and
P. parasitica
infection in both genotypes, whereas protein S-nitrosothiols were increased by
P. infestans
infection, particularly at 72 hpi related to pathogen biotrophy–necrotrophy transition. Increased levels of S-nitrosothiols localised in both proximal and distal parts to the infection site, which suggests together with their localisation to vascular bundles a signalling role in systemic responses. S-nitrosation targets in plants infected with
P. infestans
identified by a proteomic analysis include namely antioxidant and defence proteins, together with important proteins of metabolic, regulatory and structural functions. Ascorbate peroxidase S-nitrosation was observed in both genotypes in parallel to increased enzyme activity and protein level during
P. infestans
pathogenesis, namely in the susceptible genotype. These results show important regulatory functions of protein S-nitrosation in concerting molecular mechanisms of plant resistance to hemibiotrophic pathogens. |
doi_str_mv | 10.1038/s41438-021-00469-3 |
format | article |
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Solanum lycopersicum
(susceptible) and wild
Solanum habrochaites
(resistant genotype) up to 96 h post inoculation (hpi) by two hemibiotrophic oomycetes,
Phytophthora infestans
and
Phytophthora parasitica
. S-nitrosoglutathione reductase activity and protein level were decreased by
P. infestans
and
P. parasitica
infection in both genotypes, whereas protein S-nitrosothiols were increased by
P. infestans
infection, particularly at 72 hpi related to pathogen biotrophy–necrotrophy transition. Increased levels of S-nitrosothiols localised in both proximal and distal parts to the infection site, which suggests together with their localisation to vascular bundles a signalling role in systemic responses. S-nitrosation targets in plants infected with
P. infestans
identified by a proteomic analysis include namely antioxidant and defence proteins, together with important proteins of metabolic, regulatory and structural functions. Ascorbate peroxidase S-nitrosation was observed in both genotypes in parallel to increased enzyme activity and protein level during
P. infestans
pathogenesis, namely in the susceptible genotype. These results show important regulatory functions of protein S-nitrosation in concerting molecular mechanisms of plant resistance to hemibiotrophic pathogens.</description><identifier>ISSN: 2662-6810</identifier><identifier>EISSN: 2052-7276</identifier><identifier>DOI: 10.1038/s41438-021-00469-3</identifier><identifier>PMID: 33518717</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/449/2169 ; 631/449/2675 ; Agriculture ; Antioxidants ; Ascorbic acid ; Biomedical and Life Sciences ; Ecology ; Enzymatic activity ; Enzyme activity ; Genotypes ; Infections ; Inoculation ; L-Ascorbate peroxidase ; Life Sciences ; Molecular modelling ; Nitrosation ; Pathogenesis ; Pathogens ; Peroxidase ; Phytophthora infestans ; Plant Breeding/Biotechnology ; Plant Genetics and Genomics ; Plant resistance ; Plant Sciences ; Post-translation ; Protein S ; Proteins ; Reductase ; Reductases ; Signaling ; Thiols ; Tomatoes</subject><ispartof>Horticulture research, 2021-02, Vol.8 (1), Article 34</ispartof><rights>The Author(s) 2021</rights><rights>The Author(s) 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c506t-1c300b01344b5c668092cf4ca124297431483b9aa814f62601a7913822e46343</citedby><cites>FETCH-LOGICAL-c506t-1c300b01344b5c668092cf4ca124297431483b9aa814f62601a7913822e46343</cites><orcidid>0000-0003-1579-3632</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7848004/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7848004/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53770,53772</link.rule.ids></links><search><creatorcontrib>Jedelská, Tereza</creatorcontrib><creatorcontrib>Sedlářová, Michaela</creatorcontrib><creatorcontrib>Lochman, Jan</creatorcontrib><creatorcontrib>Činčalová, Lucie</creatorcontrib><creatorcontrib>Luhová, Lenka</creatorcontrib><creatorcontrib>Petřivalský, Marek</creatorcontrib><title>Protein S-nitrosation differentially modulates tomato responses to infection by hemi-biotrophic oomycetes of Phytophthora spp</title><title>Horticulture research</title><addtitle>Hortic Res</addtitle><description>Regulation of protein function by reversible S-nitrosation, a post-translational modification based on the attachment of nitroso group to cysteine thiols, has emerged among key mechanisms of NO signalling in plant development and stress responses. S-nitrosoglutathione is regarded as the most abundant low-molecular-weight S-nitrosothiol in plants, where its intracellular concentrations are modulated by S-nitrosoglutathione reductase. We analysed modulations of S-nitrosothiols and protein S-nitrosation mediated by S-nitrosoglutathione reductase in cultivated
Solanum lycopersicum
(susceptible) and wild
Solanum habrochaites
(resistant genotype) up to 96 h post inoculation (hpi) by two hemibiotrophic oomycetes,
Phytophthora infestans
and
Phytophthora parasitica
. S-nitrosoglutathione reductase activity and protein level were decreased by
P. infestans
and
P. parasitica
infection in both genotypes, whereas protein S-nitrosothiols were increased by
P. infestans
infection, particularly at 72 hpi related to pathogen biotrophy–necrotrophy transition. Increased levels of S-nitrosothiols localised in both proximal and distal parts to the infection site, which suggests together with their localisation to vascular bundles a signalling role in systemic responses. S-nitrosation targets in plants infected with
P. infestans
identified by a proteomic analysis include namely antioxidant and defence proteins, together with important proteins of metabolic, regulatory and structural functions. Ascorbate peroxidase S-nitrosation was observed in both genotypes in parallel to increased enzyme activity and protein level during
P. infestans
pathogenesis, namely in the susceptible genotype. These results show important regulatory functions of protein S-nitrosation in concerting molecular mechanisms of plant resistance to hemibiotrophic pathogens.</description><subject>631/449/2169</subject><subject>631/449/2675</subject><subject>Agriculture</subject><subject>Antioxidants</subject><subject>Ascorbic acid</subject><subject>Biomedical and Life Sciences</subject><subject>Ecology</subject><subject>Enzymatic activity</subject><subject>Enzyme activity</subject><subject>Genotypes</subject><subject>Infections</subject><subject>Inoculation</subject><subject>L-Ascorbate peroxidase</subject><subject>Life Sciences</subject><subject>Molecular modelling</subject><subject>Nitrosation</subject><subject>Pathogenesis</subject><subject>Pathogens</subject><subject>Peroxidase</subject><subject>Phytophthora infestans</subject><subject>Plant Breeding/Biotechnology</subject><subject>Plant Genetics and Genomics</subject><subject>Plant resistance</subject><subject>Plant Sciences</subject><subject>Post-translation</subject><subject>Protein S</subject><subject>Proteins</subject><subject>Reductase</subject><subject>Reductases</subject><subject>Signaling</subject><subject>Thiols</subject><subject>Tomatoes</subject><issn>2662-6810</issn><issn>2052-7276</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><recordid>eNp9kU9rHSEUxSU0NCHJF-hK6NrWq446m0AJ_QeBBpq9OD4nY5jRqfoKs-h3j3kvtHSTlXLv-R299yD0DugHoFx_LAIE14QyIJQK2RN-gs4Z7RhRTMk37S4lI1IDPUNXpTxSSqETjHfqLTrjvAOtQJ2jP3c5VR8i_kliqDkVW0OKeBfG0Wcfa7DzvOEl7fazrb7gmhZbE86-rCmWQwGHOHp3wIYNT34JZAipea1TcDilZXP-GU0jvpu22sp1Stnisq6X6HS0c_FXL-cFuv_y-f7mG7n98fX7zadb4joqKwHHKR0ocCGGzkmpac_cKJwFJlivBAeh-dBbq0GMkkkKVvXANWNeSC74Bbo-2q77YfE71-bKdjZrDovNm0k2mP87MUzmIf02SgvdttsM3r8Y5PRr70s1j2mfY_uyYUILkAwUayp2VLm2x5L9-PcFoOY5NHMMzbTQzCE0wxvEj1Bp4vjg8z_rV6gnfo6a5w</recordid><startdate>20210201</startdate><enddate>20210201</enddate><creator>Jedelská, Tereza</creator><creator>Sedlářová, Michaela</creator><creator>Lochman, Jan</creator><creator>Činčalová, Lucie</creator><creator>Luhová, Lenka</creator><creator>Petřivalský, Marek</creator><general>Nature Publishing Group UK</general><general>Oxford University Press</general><scope>C6C</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-1579-3632</orcidid></search><sort><creationdate>20210201</creationdate><title>Protein S-nitrosation differentially modulates tomato responses to infection by hemi-biotrophic oomycetes of Phytophthora spp</title><author>Jedelská, Tereza ; 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S-nitrosoglutathione is regarded as the most abundant low-molecular-weight S-nitrosothiol in plants, where its intracellular concentrations are modulated by S-nitrosoglutathione reductase. We analysed modulations of S-nitrosothiols and protein S-nitrosation mediated by S-nitrosoglutathione reductase in cultivated
Solanum lycopersicum
(susceptible) and wild
Solanum habrochaites
(resistant genotype) up to 96 h post inoculation (hpi) by two hemibiotrophic oomycetes,
Phytophthora infestans
and
Phytophthora parasitica
. S-nitrosoglutathione reductase activity and protein level were decreased by
P. infestans
and
P. parasitica
infection in both genotypes, whereas protein S-nitrosothiols were increased by
P. infestans
infection, particularly at 72 hpi related to pathogen biotrophy–necrotrophy transition. Increased levels of S-nitrosothiols localised in both proximal and distal parts to the infection site, which suggests together with their localisation to vascular bundles a signalling role in systemic responses. S-nitrosation targets in plants infected with
P. infestans
identified by a proteomic analysis include namely antioxidant and defence proteins, together with important proteins of metabolic, regulatory and structural functions. Ascorbate peroxidase S-nitrosation was observed in both genotypes in parallel to increased enzyme activity and protein level during
P. infestans
pathogenesis, namely in the susceptible genotype. These results show important regulatory functions of protein S-nitrosation in concerting molecular mechanisms of plant resistance to hemibiotrophic pathogens.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>33518717</pmid><doi>10.1038/s41438-021-00469-3</doi><orcidid>https://orcid.org/0000-0003-1579-3632</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | 631/449/2169 631/449/2675 Agriculture Antioxidants Ascorbic acid Biomedical and Life Sciences Ecology Enzymatic activity Enzyme activity Genotypes Infections Inoculation L-Ascorbate peroxidase Life Sciences Molecular modelling Nitrosation Pathogenesis Pathogens Peroxidase Phytophthora infestans Plant Breeding/Biotechnology Plant Genetics and Genomics Plant resistance Plant Sciences Post-translation Protein S Proteins Reductase Reductases Signaling Thiols Tomatoes |
title | Protein S-nitrosation differentially modulates tomato responses to infection by hemi-biotrophic oomycetes of Phytophthora spp |
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