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PoMet3 and PoMet14 associated with sulfate assimilation are essential for conidiogenesis and pathogenicity in Pyricularia oryzae
Pyricularia oryzae is the causal agent of blast disease on staple gramineous crops. Sulphur is an essential element for the biosynthesis of cysteine and methionine in fungi. Here, we targeted the P . oryzae PoMET3 encoding the enzyme ATP sulfurylase, and PoMET14 encoding the APS (adenosine-5′-phosph...
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| Published in: | Current genetics 2020-08, Vol.66 (4), p.765-774 |
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| Main Authors: | , , , , , , , , |
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| container_end_page | 774 |
| container_issue | 4 |
| container_start_page | 765 |
| container_title | Current genetics |
| container_volume | 66 |
| creator | Li, Yu Wu, Min Yu, Qin Su, Zhen-Zhu Dong, Bo Lu, Jian-Ping Lin, Fu-Cheng Liao, Qian-Sheng Liu, Xiao-Hong |
| description | Pyricularia oryzae
is the causal agent of blast disease on staple gramineous crops. Sulphur is an essential element for the biosynthesis of cysteine and methionine in fungi. Here, we targeted the
P
.
oryzae PoMET3
encoding the enzyme ATP sulfurylase, and
PoMET14
encoding the APS (adenosine-5′-phosphosulphate) kinase that are involved in sulfate assimilation and sulphur-containing amino acids biosynthesis. In
P
.
oryzae
, deletion of
PoMET3
or
PoMET14
separately results in defects of conidiophore formation, significant impairments in conidiation, methionine and cysteine auxotrophy, limited invasive hypha extension, and remarkably reduced virulence on rice and barley. Furthermore, the defects of the null mutants could be restored by supplementing with exogenous cysteine or methionine. Our study explored the biological functions of sulfur assimilation and sulphur-containing amino acids biosynthesis in
P
.
oryzae
. |
| doi_str_mv | 10.1007/s00294-020-01055-1 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_2423960534</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2423960534</sourcerecordid><originalsourceid>FETCH-LOGICAL-c375t-2af841397f4ffd44cb5a71ac5d16b97147dd01b7d8d276a3a6b32cc298b790513</originalsourceid><addsrcrecordid>eNp9kD1v2zAQhomgQeyk_QMdCgKdlR4_ZIpjYTQfQIpkSGbiRFI2A1l0SQqFM_WnR7aTduvE4917zwEPIZ8ZXDIA9S0DcC0r4FABg7qu2AmZMyl4BboRH8gcmOJVA42YkfOcnwEYb7Q6IzPBGa-llnPy5yH-9EVQHBw9lExSzDnagMU7-juUNc1j302_fT9sQo8lxIFi8tTn7IcSsKddTNTGIbgQV37wOeQDcYtlvW8EG8qOhoE-7FKwY48pII1p94L-IzntsM_-09t7QZ6ufjwub6q7--vb5fe7ygpVl4pj10gmtOpk1zkpbVujYmhrxxatVkwq54C1yjWOqwUKXLSCW8t10yoNNRMX5OuRu03x1-hzMc9xTMN00nDJhV5ALeSU4seUTTHn5DuzTWGDaWcYmL10c5RuJunmIN3s0V_e0GO78e7vyrvlKSCOgTyNhpVP_27_B_sKCn2Oeg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2423960534</pqid></control><display><type>article</type><title>PoMet3 and PoMet14 associated with sulfate assimilation are essential for conidiogenesis and pathogenicity in Pyricularia oryzae</title><source>Springer Link</source><creator>Li, Yu ; Wu, Min ; Yu, Qin ; Su, Zhen-Zhu ; Dong, Bo ; Lu, Jian-Ping ; Lin, Fu-Cheng ; Liao, Qian-Sheng ; Liu, Xiao-Hong</creator><creatorcontrib>Li, Yu ; Wu, Min ; Yu, Qin ; Su, Zhen-Zhu ; Dong, Bo ; Lu, Jian-Ping ; Lin, Fu-Cheng ; Liao, Qian-Sheng ; Liu, Xiao-Hong</creatorcontrib><description>Pyricularia oryzae
is the causal agent of blast disease on staple gramineous crops. Sulphur is an essential element for the biosynthesis of cysteine and methionine in fungi. Here, we targeted the
P
.
oryzae PoMET3
encoding the enzyme ATP sulfurylase, and
PoMET14
encoding the APS (adenosine-5′-phosphosulphate) kinase that are involved in sulfate assimilation and sulphur-containing amino acids biosynthesis. In
P
.
oryzae
, deletion of
PoMET3
or
PoMET14
separately results in defects of conidiophore formation, significant impairments in conidiation, methionine and cysteine auxotrophy, limited invasive hypha extension, and remarkably reduced virulence on rice and barley. Furthermore, the defects of the null mutants could be restored by supplementing with exogenous cysteine or methionine. Our study explored the biological functions of sulfur assimilation and sulphur-containing amino acids biosynthesis in
P
.
oryzae
.</description><identifier>ISSN: 0172-8083</identifier><identifier>EISSN: 1432-0983</identifier><identifier>DOI: 10.1007/s00294-020-01055-1</identifier><identifier>PMID: 32125494</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Adenosine ; Adenosine kinase ; Amino acids ; Ascomycota - drug effects ; Ascomycota - physiology ; Assimilation ; ATP sulfurylase ; Auxotrophy ; Biochemistry ; Biomedical and Life Sciences ; Biosynthesis ; Cell Biology ; Cysteine ; Cysteine - metabolism ; Cysteine - pharmacology ; Defects ; Fungi ; Gene Deletion ; Hordeum - microbiology ; Hyphae - pathogenicity ; Hyphae - physiology ; Kinases ; Life Sciences ; Methionine ; Methionine - metabolism ; Methionine - pharmacology ; Microbial Genetics and Genomics ; Microbiology ; Mutation ; Original Article ; Oryza - microbiology ; Pathogenicity ; Pathogens ; Phosphotransferases (Alcohol Group Acceptor) - genetics ; Phosphotransferases (Alcohol Group Acceptor) - metabolism ; Plant Diseases - microbiology ; Plant Sciences ; Proteomics ; Pyricularia oryzae ; Spores, Fungal ; Sulfate Adenylyltransferase - genetics ; Sulfate Adenylyltransferase - metabolism ; Sulfates ; Sulfur ; Virulence</subject><ispartof>Current genetics, 2020-08, Vol.66 (4), p.765-774</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2020</rights><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2020.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-2af841397f4ffd44cb5a71ac5d16b97147dd01b7d8d276a3a6b32cc298b790513</citedby><cites>FETCH-LOGICAL-c375t-2af841397f4ffd44cb5a71ac5d16b97147dd01b7d8d276a3a6b32cc298b790513</cites><orcidid>0000-0002-7466-1261</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32125494$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Yu</creatorcontrib><creatorcontrib>Wu, Min</creatorcontrib><creatorcontrib>Yu, Qin</creatorcontrib><creatorcontrib>Su, Zhen-Zhu</creatorcontrib><creatorcontrib>Dong, Bo</creatorcontrib><creatorcontrib>Lu, Jian-Ping</creatorcontrib><creatorcontrib>Lin, Fu-Cheng</creatorcontrib><creatorcontrib>Liao, Qian-Sheng</creatorcontrib><creatorcontrib>Liu, Xiao-Hong</creatorcontrib><title>PoMet3 and PoMet14 associated with sulfate assimilation are essential for conidiogenesis and pathogenicity in Pyricularia oryzae</title><title>Current genetics</title><addtitle>Curr Genet</addtitle><addtitle>Curr Genet</addtitle><description>Pyricularia oryzae
is the causal agent of blast disease on staple gramineous crops. Sulphur is an essential element for the biosynthesis of cysteine and methionine in fungi. Here, we targeted the
P
.
oryzae PoMET3
encoding the enzyme ATP sulfurylase, and
PoMET14
encoding the APS (adenosine-5′-phosphosulphate) kinase that are involved in sulfate assimilation and sulphur-containing amino acids biosynthesis. In
P
.
oryzae
, deletion of
PoMET3
or
PoMET14
separately results in defects of conidiophore formation, significant impairments in conidiation, methionine and cysteine auxotrophy, limited invasive hypha extension, and remarkably reduced virulence on rice and barley. Furthermore, the defects of the null mutants could be restored by supplementing with exogenous cysteine or methionine. Our study explored the biological functions of sulfur assimilation and sulphur-containing amino acids biosynthesis in
P
.
oryzae
.</description><subject>Adenosine</subject><subject>Adenosine kinase</subject><subject>Amino acids</subject><subject>Ascomycota - drug effects</subject><subject>Ascomycota - physiology</subject><subject>Assimilation</subject><subject>ATP sulfurylase</subject><subject>Auxotrophy</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biosynthesis</subject><subject>Cell Biology</subject><subject>Cysteine</subject><subject>Cysteine - metabolism</subject><subject>Cysteine - pharmacology</subject><subject>Defects</subject><subject>Fungi</subject><subject>Gene Deletion</subject><subject>Hordeum - microbiology</subject><subject>Hyphae - pathogenicity</subject><subject>Hyphae - physiology</subject><subject>Kinases</subject><subject>Life Sciences</subject><subject>Methionine</subject><subject>Methionine - metabolism</subject><subject>Methionine - pharmacology</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Mutation</subject><subject>Original Article</subject><subject>Oryza - microbiology</subject><subject>Pathogenicity</subject><subject>Pathogens</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - genetics</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - metabolism</subject><subject>Plant Diseases - microbiology</subject><subject>Plant Sciences</subject><subject>Proteomics</subject><subject>Pyricularia oryzae</subject><subject>Spores, Fungal</subject><subject>Sulfate Adenylyltransferase - genetics</subject><subject>Sulfate Adenylyltransferase - metabolism</subject><subject>Sulfates</subject><subject>Sulfur</subject><subject>Virulence</subject><issn>0172-8083</issn><issn>1432-0983</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNp9kD1v2zAQhomgQeyk_QMdCgKdlR4_ZIpjYTQfQIpkSGbiRFI2A1l0SQqFM_WnR7aTduvE4917zwEPIZ8ZXDIA9S0DcC0r4FABg7qu2AmZMyl4BboRH8gcmOJVA42YkfOcnwEYb7Q6IzPBGa-llnPy5yH-9EVQHBw9lExSzDnagMU7-juUNc1j302_fT9sQo8lxIFi8tTn7IcSsKddTNTGIbgQV37wOeQDcYtlvW8EG8qOhoE-7FKwY48pII1p94L-IzntsM_-09t7QZ6ufjwub6q7--vb5fe7ygpVl4pj10gmtOpk1zkpbVujYmhrxxatVkwq54C1yjWOqwUKXLSCW8t10yoNNRMX5OuRu03x1-hzMc9xTMN00nDJhV5ALeSU4seUTTHn5DuzTWGDaWcYmL10c5RuJunmIN3s0V_e0GO78e7vyrvlKSCOgTyNhpVP_27_B_sKCn2Oeg</recordid><startdate>20200801</startdate><enddate>20200801</enddate><creator>Li, Yu</creator><creator>Wu, Min</creator><creator>Yu, Qin</creator><creator>Su, Zhen-Zhu</creator><creator>Dong, Bo</creator><creator>Lu, Jian-Ping</creator><creator>Lin, Fu-Cheng</creator><creator>Liao, Qian-Sheng</creator><creator>Liu, Xiao-Hong</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><orcidid>https://orcid.org/0000-0002-7466-1261</orcidid></search><sort><creationdate>20200801</creationdate><title>PoMet3 and PoMet14 associated with sulfate assimilation are essential for conidiogenesis and pathogenicity in Pyricularia oryzae</title><author>Li, Yu ; Wu, Min ; Yu, Qin ; Su, Zhen-Zhu ; Dong, Bo ; Lu, Jian-Ping ; Lin, Fu-Cheng ; Liao, Qian-Sheng ; Liu, Xiao-Hong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-2af841397f4ffd44cb5a71ac5d16b97147dd01b7d8d276a3a6b32cc298b790513</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Adenosine</topic><topic>Adenosine kinase</topic><topic>Amino acids</topic><topic>Ascomycota - drug effects</topic><topic>Ascomycota - physiology</topic><topic>Assimilation</topic><topic>ATP sulfurylase</topic><topic>Auxotrophy</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biosynthesis</topic><topic>Cell Biology</topic><topic>Cysteine</topic><topic>Cysteine - metabolism</topic><topic>Cysteine - pharmacology</topic><topic>Defects</topic><topic>Fungi</topic><topic>Gene Deletion</topic><topic>Hordeum - microbiology</topic><topic>Hyphae - pathogenicity</topic><topic>Hyphae - physiology</topic><topic>Kinases</topic><topic>Life Sciences</topic><topic>Methionine</topic><topic>Methionine - metabolism</topic><topic>Methionine - pharmacology</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Mutation</topic><topic>Original Article</topic><topic>Oryza - microbiology</topic><topic>Pathogenicity</topic><topic>Pathogens</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - genetics</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - metabolism</topic><topic>Plant Diseases - microbiology</topic><topic>Plant Sciences</topic><topic>Proteomics</topic><topic>Pyricularia oryzae</topic><topic>Spores, Fungal</topic><topic>Sulfate Adenylyltransferase - genetics</topic><topic>Sulfate Adenylyltransferase - metabolism</topic><topic>Sulfates</topic><topic>Sulfur</topic><topic>Virulence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Yu</creatorcontrib><creatorcontrib>Wu, Min</creatorcontrib><creatorcontrib>Yu, Qin</creatorcontrib><creatorcontrib>Su, Zhen-Zhu</creatorcontrib><creatorcontrib>Dong, Bo</creatorcontrib><creatorcontrib>Lu, Jian-Ping</creatorcontrib><creatorcontrib>Lin, Fu-Cheng</creatorcontrib><creatorcontrib>Liao, Qian-Sheng</creatorcontrib><creatorcontrib>Liu, Xiao-Hong</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection (Proquest)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><jtitle>Current genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Yu</au><au>Wu, Min</au><au>Yu, Qin</au><au>Su, Zhen-Zhu</au><au>Dong, Bo</au><au>Lu, Jian-Ping</au><au>Lin, Fu-Cheng</au><au>Liao, Qian-Sheng</au><au>Liu, Xiao-Hong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PoMet3 and PoMet14 associated with sulfate assimilation are essential for conidiogenesis and pathogenicity in Pyricularia oryzae</atitle><jtitle>Current genetics</jtitle><stitle>Curr Genet</stitle><addtitle>Curr Genet</addtitle><date>2020-08-01</date><risdate>2020</risdate><volume>66</volume><issue>4</issue><spage>765</spage><epage>774</epage><pages>765-774</pages><issn>0172-8083</issn><eissn>1432-0983</eissn><abstract>Pyricularia oryzae
is the causal agent of blast disease on staple gramineous crops. Sulphur is an essential element for the biosynthesis of cysteine and methionine in fungi. Here, we targeted the
P
.
oryzae PoMET3
encoding the enzyme ATP sulfurylase, and
PoMET14
encoding the APS (adenosine-5′-phosphosulphate) kinase that are involved in sulfate assimilation and sulphur-containing amino acids biosynthesis. In
P
.
oryzae
, deletion of
PoMET3
or
PoMET14
separately results in defects of conidiophore formation, significant impairments in conidiation, methionine and cysteine auxotrophy, limited invasive hypha extension, and remarkably reduced virulence on rice and barley. Furthermore, the defects of the null mutants could be restored by supplementing with exogenous cysteine or methionine. Our study explored the biological functions of sulfur assimilation and sulphur-containing amino acids biosynthesis in
P
.
oryzae
.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>32125494</pmid><doi>10.1007/s00294-020-01055-1</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-7466-1261</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0172-8083 |
| ispartof | Current genetics, 2020-08, Vol.66 (4), p.765-774 |
| issn | 0172-8083 1432-0983 |
| language | eng |
| recordid | cdi_proquest_journals_2423960534 |
| source | Springer Link |
| subjects | Adenosine Adenosine kinase Amino acids Ascomycota - drug effects Ascomycota - physiology Assimilation ATP sulfurylase Auxotrophy Biochemistry Biomedical and Life Sciences Biosynthesis Cell Biology Cysteine Cysteine - metabolism Cysteine - pharmacology Defects Fungi Gene Deletion Hordeum - microbiology Hyphae - pathogenicity Hyphae - physiology Kinases Life Sciences Methionine Methionine - metabolism Methionine - pharmacology Microbial Genetics and Genomics Microbiology Mutation Original Article Oryza - microbiology Pathogenicity Pathogens Phosphotransferases (Alcohol Group Acceptor) - genetics Phosphotransferases (Alcohol Group Acceptor) - metabolism Plant Diseases - microbiology Plant Sciences Proteomics Pyricularia oryzae Spores, Fungal Sulfate Adenylyltransferase - genetics Sulfate Adenylyltransferase - metabolism Sulfates Sulfur Virulence |
| title | PoMet3 and PoMet14 associated with sulfate assimilation are essential for conidiogenesis and pathogenicity in Pyricularia oryzae |
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