Shuzhen Deng, Lin Xu, Zhe Xu, Wuyun Lv, Zhengxian Chen, Nan Yang, Nicholas J. Talbot, Zhengyi Wang
{"title":"据推测，PKA磷酸化位点S227在水稻大孔霉感染相关的形态发生和致病性中是必不可少的","authors":"Shuzhen Deng, Lin Xu, Zhe Xu, Wuyun Lv, Zhengxian Chen, Nan Yang, Nicholas J. Talbot, Zhengyi Wang","doi":"10.1111/cmi.13370","DOIUrl":null,"url":null,"abstract":"<div>\n \n \n <section>\n \n <p>In the rice blast fungus <i>Magnaporthe oryzae</i>, the cAMP signalling pathway plays a critical role in regulating leaf surface recognition and the initiation of appressorium development. Direct downstream targets of the cAMP signalling pathway are, however, not well-characterised. The MoSom1 protein functions downstream of the cAMP dependent protein kinase A (cAMP-PKA) and is essential for infection-related morphogenesis and pathogenicity. In this study, we show that mutation of a putative PKA phosphorylation site in MoSom1 is essential for its role in appressorium differentiation and pathogenicity in <i>M. oryzae</i>. Mutation of serine 227 in MoSom1 by deletion or serine (S) substitution to alanine (A), valine (V) or tyrosine (Y), resulted in defects of conidiation, appressorium-like structure formation and fungal pathogenicity. Western blot analysis confirmed that S227 in MoSom1 is a putative PKA phosphorylation site. Furthermore, a <i>ΔMosom1</i> mutant showed reduced expression of <i>PMK1</i> and was defective in Pmk1 phosphorylation, indicating that the Pmk1 mitogen-activated protein kinase (MAPK) acts downstream of MoSom1 in <i>M. oryzae</i>. We conclude that the cAMP-PKA pathway may regulate the Pmk1 MAPK pathway through MoSom1 during rice infection by the blast fungus.</p>\n </section>\n \n <section>\n \n <h3> Take Aways</h3>\n \n <div>\n <ul>\n \n <li>S227 is crucial for MoSom1 function in <i>M. oryzae</i>.</li>\n \n <li>S227 in MoSom1 was identified as a putative PKA phosphorylation site in <i>M. oryzae</i>.</li>\n \n <li>S227 is essential for infection-related morphogenesis and pathogenicity in <i>M. oryzae</i>.</li>\n </ul>\n </div>\n </section>\n </div>","PeriodicalId":2,"journal":{"name":"ACS Applied Bio Materials","volume":null,"pages":null},"PeriodicalIF":4.6000,"publicationDate":"2021-06-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/cmi.13370","citationCount":"2","resultStr":"{\"title\":\"A putative PKA phosphorylation site S227 in MoSom1 is essential for infection-related morphogenesis and pathogenicity in Magnaporthe oryzae\",\"authors\":\"Shuzhen Deng, Lin Xu, Zhe Xu, Wuyun Lv, Zhengxian Chen, Nan Yang, Nicholas J. Talbot, Zhengyi Wang\",\"doi\":\"10.1111/cmi.13370\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div>\\n \\n \\n <section>\\n \\n <p>In the rice blast fungus <i>Magnaporthe oryzae</i>, the cAMP signalling pathway plays a critical role in regulating leaf surface recognition and the initiation of appressorium development. Direct downstream targets of the cAMP signalling pathway are, however, not well-characterised. The MoSom1 protein functions downstream of the cAMP dependent protein kinase A (cAMP-PKA) and is essential for infection-related morphogenesis and pathogenicity. In this study, we show that mutation of a putative PKA phosphorylation site in MoSom1 is essential for its role in appressorium differentiation and pathogenicity in <i>M. oryzae</i>. Mutation of serine 227 in MoSom1 by deletion or serine (S) substitution to alanine (A), valine (V) or tyrosine (Y), resulted in defects of conidiation, appressorium-like structure formation and fungal pathogenicity. Western blot analysis confirmed that S227 in MoSom1 is a putative PKA phosphorylation site. Furthermore, a <i>ΔMosom1</i> mutant showed reduced expression of <i>PMK1</i> and was defective in Pmk1 phosphorylation, indicating that the Pmk1 mitogen-activated protein kinase (MAPK) acts downstream of MoSom1 in <i>M. oryzae</i>. We conclude that the cAMP-PKA pathway may regulate the Pmk1 MAPK pathway through MoSom1 during rice infection by the blast fungus.</p>\\n </section>\\n \\n <section>\\n \\n <h3> Take Aways</h3>\\n \\n <div>\\n <ul>\\n \\n <li>S227 is crucial for MoSom1 function in <i>M. oryzae</i>.</li>\\n \\n <li>S227 in MoSom1 was identified as a putative PKA phosphorylation site in <i>M. oryzae</i>.</li>\\n \\n <li>S227 is essential for infection-related morphogenesis and pathogenicity in <i>M. oryzae</i>.</li>\\n </ul>\\n </div>\\n </section>\\n </div>\",\"PeriodicalId\":2,\"journal\":{\"name\":\"ACS Applied Bio Materials\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":4.6000,\"publicationDate\":\"2021-06-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1111/cmi.13370\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"ACS Applied Bio Materials\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1111/cmi.13370\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"MATERIALS SCIENCE, BIOMATERIALS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"ACS Applied Bio Materials","FirstCategoryId":"99","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1111/cmi.13370","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"MATERIALS SCIENCE, BIOMATERIALS","Score":null,"Total":0}
A putative PKA phosphorylation site S227 in MoSom1 is essential for infection-related morphogenesis and pathogenicity in Magnaporthe oryzae
In the rice blast fungus Magnaporthe oryzae, the cAMP signalling pathway plays a critical role in regulating leaf surface recognition and the initiation of appressorium development. Direct downstream targets of the cAMP signalling pathway are, however, not well-characterised. The MoSom1 protein functions downstream of the cAMP dependent protein kinase A (cAMP-PKA) and is essential for infection-related morphogenesis and pathogenicity. In this study, we show that mutation of a putative PKA phosphorylation site in MoSom1 is essential for its role in appressorium differentiation and pathogenicity in M. oryzae. Mutation of serine 227 in MoSom1 by deletion or serine (S) substitution to alanine (A), valine (V) or tyrosine (Y), resulted in defects of conidiation, appressorium-like structure formation and fungal pathogenicity. Western blot analysis confirmed that S227 in MoSom1 is a putative PKA phosphorylation site. Furthermore, a ΔMosom1 mutant showed reduced expression of PMK1 and was defective in Pmk1 phosphorylation, indicating that the Pmk1 mitogen-activated protein kinase (MAPK) acts downstream of MoSom1 in M. oryzae. We conclude that the cAMP-PKA pathway may regulate the Pmk1 MAPK pathway through MoSom1 during rice infection by the blast fungus.
Take Aways
S227 is crucial for MoSom1 function in M. oryzae.
S227 in MoSom1 was identified as a putative PKA phosphorylation site in M. oryzae.
S227 is essential for infection-related morphogenesis and pathogenicity in M. oryzae.
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