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Sir2‐mediated cytoplasmic deacetylation facilitates pathogenic fungi infection in host plants
Summary Lysine acetylation is an evolutionarily conserved and widespread post‐translational modification implicated in the regulation of multiple metabolic processes, but its function remains largely unknown in plant pathogenic fungi. A comprehensive analysis combined with proteomic, molecular and c...
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| Published in: | The New phytologist 2024-02, Vol.241 (4), p.1732-1746 |
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| Main Authors: | , , , , |
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| container_end_page | 1746 |
| container_issue | 4 |
| container_start_page | 1732 |
| container_title | The New phytologist |
| container_volume | 241 |
| creator | Zhang, Ning Hu, Jicheng Liu, Zhishan Liang, Wenxing Song, Limin |
| description | Summary
Lysine acetylation is an evolutionarily conserved and widespread post‐translational modification implicated in the regulation of multiple metabolic processes, but its function remains largely unknown in plant pathogenic fungi.
A comprehensive analysis combined with proteomic, molecular and cellular approaches was presented to explore the roles of cytoplasmic acetylation in Fusarium oxsysporum f.sp. lycopersici (Fol).
The divergent cytoplasmic deacetylase FolSir2 was biochemically characterized, which is contributing to fungal virulence. Based on this, a total of 1752 acetylated sites in 897 proteins were identified in Fol via LC–MS/MS analysis. Further analyses of the quantitative acetylome revealed that 115 proteins representing two major pathways, translational and ribosome biogenesis, were hyperacetylated in the ∆Folsir2 strain. We experimentally examined the regulatory roles of FolSir2 on K271 deacetylation of FolGsk3, a serine/tyrosine kinase implicated in a variety of cellular functions, which was found to be crucial for the activation of FolGsk3 and thus modulated Fol pathogenicity. Cytoplasmic deacetylation by FolSir2 homologues has a similar function in Botrytis cinerea and likely other fungal pathogens.
These findings reveal a conserved mechanism of silent information regulator 2‐mediated cytoplasmic deacetylation that is involved in plant‐fungal pathogenicity, providing a candidate target for designing broad‐spectrum fungicides to control plant diseases. |
| doi_str_mv | 10.1111/nph.19438 |
| format | article |
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Lysine acetylation is an evolutionarily conserved and widespread post‐translational modification implicated in the regulation of multiple metabolic processes, but its function remains largely unknown in plant pathogenic fungi.
A comprehensive analysis combined with proteomic, molecular and cellular approaches was presented to explore the roles of cytoplasmic acetylation in Fusarium oxsysporum f.sp. lycopersici (Fol).
The divergent cytoplasmic deacetylase FolSir2 was biochemically characterized, which is contributing to fungal virulence. Based on this, a total of 1752 acetylated sites in 897 proteins were identified in Fol via LC–MS/MS analysis. Further analyses of the quantitative acetylome revealed that 115 proteins representing two major pathways, translational and ribosome biogenesis, were hyperacetylated in the ∆Folsir2 strain. We experimentally examined the regulatory roles of FolSir2 on K271 deacetylation of FolGsk3, a serine/tyrosine kinase implicated in a variety of cellular functions, which was found to be crucial for the activation of FolGsk3 and thus modulated Fol pathogenicity. Cytoplasmic deacetylation by FolSir2 homologues has a similar function in Botrytis cinerea and likely other fungal pathogens.
These findings reveal a conserved mechanism of silent information regulator 2‐mediated cytoplasmic deacetylation that is involved in plant‐fungal pathogenicity, providing a candidate target for designing broad‐spectrum fungicides to control plant diseases.</description><identifier>ISSN: 0028-646X</identifier><identifier>EISSN: 1469-8137</identifier><identifier>DOI: 10.1111/nph.19438</identifier><identifier>PMID: 38037458</identifier><language>eng</language><publisher>England: Wiley Subscription Services, Inc</publisher><subject>Acetylation ; Biogenesis ; Chromatography, Liquid ; deacetylase ; Deacetylation ; fungal infection ; Fungi ; Fungicides ; Fusarium ; Fusarium oxysporum ; Host plants ; Kinases ; Lysine ; lysine acetylation ; Pathogenicity ; Pathogens ; Plant diseases ; Plant Diseases - microbiology ; Plants ; post‐translational modification ; Protein Processing, Post-Translational ; Proteins ; Proteomics ; Ribosomes ; Serine ; Tandem Mass Spectrometry ; Translation ; Tyrosine ; Virulence</subject><ispartof>The New phytologist, 2024-02, Vol.241 (4), p.1732-1746</ispartof><rights>2023 The Authors © 2023 New Phytologist Foundation</rights><rights>2023 The Authors New Phytologist © 2023 New Phytologist Foundation.</rights><rights>Copyright © 2024 New Phytologist Trust</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c3488-f5f459e12ade1c68b45d170e8137b505a29968a667968b1fc1fe677ac20f9a53</cites><orcidid>0000-0002-3791-4901 ; 0000-0002-4824-3795</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38037458$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Ning</creatorcontrib><creatorcontrib>Hu, Jicheng</creatorcontrib><creatorcontrib>Liu, Zhishan</creatorcontrib><creatorcontrib>Liang, Wenxing</creatorcontrib><creatorcontrib>Song, Limin</creatorcontrib><title>Sir2‐mediated cytoplasmic deacetylation facilitates pathogenic fungi infection in host plants</title><title>The New phytologist</title><addtitle>New Phytol</addtitle><description>Summary
Lysine acetylation is an evolutionarily conserved and widespread post‐translational modification implicated in the regulation of multiple metabolic processes, but its function remains largely unknown in plant pathogenic fungi.
A comprehensive analysis combined with proteomic, molecular and cellular approaches was presented to explore the roles of cytoplasmic acetylation in Fusarium oxsysporum f.sp. lycopersici (Fol).
The divergent cytoplasmic deacetylase FolSir2 was biochemically characterized, which is contributing to fungal virulence. Based on this, a total of 1752 acetylated sites in 897 proteins were identified in Fol via LC–MS/MS analysis. Further analyses of the quantitative acetylome revealed that 115 proteins representing two major pathways, translational and ribosome biogenesis, were hyperacetylated in the ∆Folsir2 strain. We experimentally examined the regulatory roles of FolSir2 on K271 deacetylation of FolGsk3, a serine/tyrosine kinase implicated in a variety of cellular functions, which was found to be crucial for the activation of FolGsk3 and thus modulated Fol pathogenicity. Cytoplasmic deacetylation by FolSir2 homologues has a similar function in Botrytis cinerea and likely other fungal pathogens.
These findings reveal a conserved mechanism of silent information regulator 2‐mediated cytoplasmic deacetylation that is involved in plant‐fungal pathogenicity, providing a candidate target for designing broad‐spectrum fungicides to control plant diseases.</description><subject>Acetylation</subject><subject>Biogenesis</subject><subject>Chromatography, Liquid</subject><subject>deacetylase</subject><subject>Deacetylation</subject><subject>fungal infection</subject><subject>Fungi</subject><subject>Fungicides</subject><subject>Fusarium</subject><subject>Fusarium oxysporum</subject><subject>Host plants</subject><subject>Kinases</subject><subject>Lysine</subject><subject>lysine acetylation</subject><subject>Pathogenicity</subject><subject>Pathogens</subject><subject>Plant diseases</subject><subject>Plant Diseases - microbiology</subject><subject>Plants</subject><subject>post‐translational modification</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Ribosomes</subject><subject>Serine</subject><subject>Tandem Mass Spectrometry</subject><subject>Translation</subject><subject>Tyrosine</subject><subject>Virulence</subject><issn>0028-646X</issn><issn>1469-8137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><recordid>eNp10DFOwzAUBmALgWgpDFwARWKBIa3tJI49ogooUgVIdGCzHMduXaVJiB2hbByBM3IS3KYwIOHlLd_79fwDcI7gGPk3KevVGLE4ogdgiGLCQoqi9BAMIcQ0JDF5HYATa9cQQpYQfAwGEYVRGid0CPiLafDXx-dG5UY4lQeyc1VdCLsxMsiVkMp1hXCmKgMtpCmM88oGtXCraqlKj3RbLk1gSq3kjpkyWFXWBT6kdPYUHGlRWHW2nyOwuLtdTGfh_On-YXozD2UUUxrqRMcJUwiLXCFJaBYnOUqh2n4kS2AiMGOECkJSPzKkJdKKpKmQGGomkmgErvrYuqneWmUd3xgrVeFvUFVrOaZ-D2KCI08v_9B11TalP45jhlJGKYHIq-teyaaytlGa143ZiKbjCPJt6dyXznele3uxT2wz3-Ov_GnZg0kP3k2huv-T-OPzrI_8BoyYjQk</recordid><startdate>202402</startdate><enddate>202402</enddate><creator>Zhang, Ning</creator><creator>Hu, Jicheng</creator><creator>Liu, Zhishan</creator><creator>Liang, Wenxing</creator><creator>Song, Limin</creator><general>Wiley Subscription Services, Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7SN</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-3791-4901</orcidid><orcidid>https://orcid.org/0000-0002-4824-3795</orcidid></search><sort><creationdate>202402</creationdate><title>Sir2‐mediated cytoplasmic deacetylation facilitates pathogenic fungi infection in host plants</title><author>Zhang, Ning ; Hu, Jicheng ; Liu, Zhishan ; Liang, Wenxing ; Song, Limin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3488-f5f459e12ade1c68b45d170e8137b505a29968a667968b1fc1fe677ac20f9a53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Acetylation</topic><topic>Biogenesis</topic><topic>Chromatography, Liquid</topic><topic>deacetylase</topic><topic>Deacetylation</topic><topic>fungal infection</topic><topic>Fungi</topic><topic>Fungicides</topic><topic>Fusarium</topic><topic>Fusarium oxysporum</topic><topic>Host plants</topic><topic>Kinases</topic><topic>Lysine</topic><topic>lysine acetylation</topic><topic>Pathogenicity</topic><topic>Pathogens</topic><topic>Plant diseases</topic><topic>Plant Diseases - microbiology</topic><topic>Plants</topic><topic>post‐translational modification</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>Ribosomes</topic><topic>Serine</topic><topic>Tandem Mass Spectrometry</topic><topic>Translation</topic><topic>Tyrosine</topic><topic>Virulence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Ning</creatorcontrib><creatorcontrib>Hu, Jicheng</creatorcontrib><creatorcontrib>Liu, Zhishan</creatorcontrib><creatorcontrib>Liang, Wenxing</creatorcontrib><creatorcontrib>Song, Limin</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Ecology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The New phytologist</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Ning</au><au>Hu, Jicheng</au><au>Liu, Zhishan</au><au>Liang, Wenxing</au><au>Song, Limin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sir2‐mediated cytoplasmic deacetylation facilitates pathogenic fungi infection in host plants</atitle><jtitle>The New phytologist</jtitle><addtitle>New Phytol</addtitle><date>2024-02</date><risdate>2024</risdate><volume>241</volume><issue>4</issue><spage>1732</spage><epage>1746</epage><pages>1732-1746</pages><issn>0028-646X</issn><eissn>1469-8137</eissn><abstract>Summary
Lysine acetylation is an evolutionarily conserved and widespread post‐translational modification implicated in the regulation of multiple metabolic processes, but its function remains largely unknown in plant pathogenic fungi.
A comprehensive analysis combined with proteomic, molecular and cellular approaches was presented to explore the roles of cytoplasmic acetylation in Fusarium oxsysporum f.sp. lycopersici (Fol).
The divergent cytoplasmic deacetylase FolSir2 was biochemically characterized, which is contributing to fungal virulence. Based on this, a total of 1752 acetylated sites in 897 proteins were identified in Fol via LC–MS/MS analysis. Further analyses of the quantitative acetylome revealed that 115 proteins representing two major pathways, translational and ribosome biogenesis, were hyperacetylated in the ∆Folsir2 strain. We experimentally examined the regulatory roles of FolSir2 on K271 deacetylation of FolGsk3, a serine/tyrosine kinase implicated in a variety of cellular functions, which was found to be crucial for the activation of FolGsk3 and thus modulated Fol pathogenicity. Cytoplasmic deacetylation by FolSir2 homologues has a similar function in Botrytis cinerea and likely other fungal pathogens.
These findings reveal a conserved mechanism of silent information regulator 2‐mediated cytoplasmic deacetylation that is involved in plant‐fungal pathogenicity, providing a candidate target for designing broad‐spectrum fungicides to control plant diseases.</abstract><cop>England</cop><pub>Wiley Subscription Services, Inc</pub><pmid>38037458</pmid><doi>10.1111/nph.19438</doi><tpages>1746</tpages><orcidid>https://orcid.org/0000-0002-3791-4901</orcidid><orcidid>https://orcid.org/0000-0002-4824-3795</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Acetylation Biogenesis Chromatography, Liquid deacetylase Deacetylation fungal infection Fungi Fungicides Fusarium Fusarium oxysporum Host plants Kinases Lysine lysine acetylation Pathogenicity Pathogens Plant diseases Plant Diseases - microbiology Plants post‐translational modification Protein Processing, Post-Translational Proteins Proteomics Ribosomes Serine Tandem Mass Spectrometry Translation Tyrosine Virulence |
| title | Sir2‐mediated cytoplasmic deacetylation facilitates pathogenic fungi infection in host plants |
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