Identification and characterization of a sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans
The amino acid biosynthetic pathway of invasive pathogenic fungi has been studied as a potential antifungal drug target. Studies of the disruption of genes involved in amino acid biosynthesis have demonstrated the importance of this pathway in the virulence of Cryptococcus neoformans . Here, we iden...
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| Veröffentlicht in: | Current genetics 2021-02, Vol.67 (1), p.115-128 |
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| creator | Nguyen, Phuong-Thao Toh-e, Akio Nguyen, Ngoc-Hung Imanishi-Shimizu, Yumi Watanabe, Akira Kamei, Katsuhiko Shimizu, Kiminori |
| description | The amino acid biosynthetic pathway of invasive pathogenic fungi has been studied as a potential antifungal drug target. Studies of the disruption of genes involved in amino acid biosynthesis have demonstrated the importance of this pathway in the virulence of
Cryptococcus neoformans
. Here, we identified the
MET5
(
CNL05500
) and
MET10
(
CNG03990
) genes in this pathway, both encoding sulfite reductase, which catalyzes the reduction of sulfite to sulfide. The
MET14
(
CNE03880
) gene was also identified, which is responsible for the conversion of sulfate to sulfite. The use of cysteine as a sulfur source led to the production of methionine via hydrogen sulfide synthesis mediated by
CYS4
(
CNA06170
)
, CYS3
(
CNN01730
), and
MST1
(
CND03690
).
MST1
exhibited high homology with the
TUM1
gene of
Saccharomyces cerevisiae
, which has functional similarity with the 3-mercaptopyruvate sulfurtransferase (
3-MST
) gene in humans. Although the hypothesis that hydrogen sulfide is produced from cysteine via
CYS4
,
CYS3
, and
MST1
warrants further study, the new insight into the metabolic pathway of sulfur-containing amino acids in
C. neoformans
provided here indicates the usefulness of this system in the development of screening tools for antifungal drug agents. |
| doi_str_mv | 10.1007/s00294-020-01112-9 |
| format | Article |
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Cryptococcus neoformans
. Here, we identified the
MET5
(
CNL05500
) and
MET10
(
CNG03990
) genes in this pathway, both encoding sulfite reductase, which catalyzes the reduction of sulfite to sulfide. The
MET14
(
CNE03880
) gene was also identified, which is responsible for the conversion of sulfate to sulfite. The use of cysteine as a sulfur source led to the production of methionine via hydrogen sulfide synthesis mediated by
CYS4
(
CNA06170
)
, CYS3
(
CNN01730
), and
MST1
(
CND03690
).
MST1
exhibited high homology with the
TUM1
gene of
Saccharomyces cerevisiae
, which has functional similarity with the 3-mercaptopyruvate sulfurtransferase (
3-MST
) gene in humans. Although the hypothesis that hydrogen sulfide is produced from cysteine via
CYS4
,
CYS3
, and
MST1
warrants further study, the new insight into the metabolic pathway of sulfur-containing amino acids in
C. neoformans
provided here indicates the usefulness of this system in the development of screening tools for antifungal drug agents.</description><identifier>ISSN: 0172-8083</identifier><identifier>EISSN: 1432-0983</identifier><identifier>DOI: 10.1007/s00294-020-01112-9</identifier><identifier>PMID: 33001274</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>3-Mercaptopyruvate sulfurtransferase ; Amino acids ; Antifungal agents ; Biochemistry ; Biomedical and Life Sciences ; Biosynthesis ; Cell Biology ; Cryptococcus neoformans ; Cysteine ; Fungal infections ; Fungi ; Fungicides ; Genes ; Homology ; Hydrogen sulfide ; Life Sciences ; Metabolic pathways ; Methionine ; Microbial Genetics and Genomics ; Microbiology ; Original Article ; Plant Sciences ; Proteomics ; Reductases ; Sulfite ; Sulfite reductase ; Sulfur ; Sulfurtransferase ; Therapeutic targets ; Virulence ; Yeasts</subject><ispartof>Current genetics, 2021-02, Vol.67 (1), p.115-128</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-c3569-58fe02d9e952d506b6fcf82bceecf88eded457579d91a373af82657c90de266c3</citedby><cites>FETCH-LOGICAL-c3569-58fe02d9e952d506b6fcf82bceecf88eded457579d91a373af82657c90de266c3</cites><orcidid>0000-0001-5966-976X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00294-020-01112-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00294-020-01112-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33001274$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nguyen, Phuong-Thao</creatorcontrib><creatorcontrib>Toh-e, Akio</creatorcontrib><creatorcontrib>Nguyen, Ngoc-Hung</creatorcontrib><creatorcontrib>Imanishi-Shimizu, Yumi</creatorcontrib><creatorcontrib>Watanabe, Akira</creatorcontrib><creatorcontrib>Kamei, Katsuhiko</creatorcontrib><creatorcontrib>Shimizu, Kiminori</creatorcontrib><title>Identification and characterization of a sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans</title><title>Current genetics</title><addtitle>Curr Genet</addtitle><addtitle>Curr Genet</addtitle><description>The amino acid biosynthetic pathway of invasive pathogenic fungi has been studied as a potential antifungal drug target. Studies of the disruption of genes involved in amino acid biosynthesis have demonstrated the importance of this pathway in the virulence of
Cryptococcus neoformans
. Here, we identified the
MET5
(
CNL05500
) and
MET10
(
CNG03990
) genes in this pathway, both encoding sulfite reductase, which catalyzes the reduction of sulfite to sulfide. The
MET14
(
CNE03880
) gene was also identified, which is responsible for the conversion of sulfate to sulfite. The use of cysteine as a sulfur source led to the production of methionine via hydrogen sulfide synthesis mediated by
CYS4
(
CNA06170
)
, CYS3
(
CNN01730
), and
MST1
(
CND03690
).
MST1
exhibited high homology with the
TUM1
gene of
Saccharomyces cerevisiae
, which has functional similarity with the 3-mercaptopyruvate sulfurtransferase (
3-MST
) gene in humans. Although the hypothesis that hydrogen sulfide is produced from cysteine via
CYS4
,
CYS3
, and
MST1
warrants further study, the new insight into the metabolic pathway of sulfur-containing amino acids in
C. neoformans
provided here indicates the usefulness of this system in the development of screening tools for antifungal drug agents.</description><subject>3-Mercaptopyruvate sulfurtransferase</subject><subject>Amino acids</subject><subject>Antifungal agents</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biosynthesis</subject><subject>Cell Biology</subject><subject>Cryptococcus neoformans</subject><subject>Cysteine</subject><subject>Fungal infections</subject><subject>Fungi</subject><subject>Fungicides</subject><subject>Genes</subject><subject>Homology</subject><subject>Hydrogen sulfide</subject><subject>Life Sciences</subject><subject>Metabolic pathways</subject><subject>Methionine</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Original Article</subject><subject>Plant Sciences</subject><subject>Proteomics</subject><subject>Reductases</subject><subject>Sulfite</subject><subject>Sulfite reductase</subject><subject>Sulfur</subject><subject>Sulfurtransferase</subject><subject>Therapeutic targets</subject><subject>Virulence</subject><subject>Yeasts</subject><issn>0172-8083</issn><issn>1432-0983</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp9kc-KFDEQxoMo7rj6Ah4k4MVLa_50d5KjDKsuLHjRc0gn1T1ZupMxSSPjq_lyZqZXBQ-eKtT3-6qKfAi9pOQtJUS8y4Qw1TaEkYZQSlmjHqEdbTlriJL8MdoRKlgjieRX6FnO94RQJpV4iq44P79Fu0M_bx2E4kdvTfExYBMctgeTjC2Q_I-tGUdscF7n0RfACdxqi8mAJwhwMQT4jn3IfjqUXPXJJOfDhMsBLq41NTaGYnw4d83iQ8TGeocXKGaIs89LtV_wwWTvfFxOFkpcMz6ByQXv0-lYoo3W1laAOMa0mJCfoyejmTO8eKjX6OuHmy_7T83d54-3-_d3jeVdr5pOjkCYU6A65jrSD_1oR8kGC1CrBAeu7UQnlFPUcMFNFftOWEUcsL63_Bq92eYeU_y2Qi568dnCPJt6y5o1a1sh2_q3bUVf_4PexzWFel2lpFJEduJMsY2yKeacYNTH5BeTTpoSfY5Wb9HqGq2-RKtVNb16GL0OC7g_lt9ZVoBvQK5SmCD93f2fsb8ApUW0Mg</recordid><startdate>20210201</startdate><enddate>20210201</enddate><creator>Nguyen, 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and characterization of a sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans</title><author>Nguyen, Phuong-Thao ; Toh-e, Akio ; Nguyen, Ngoc-Hung ; Imanishi-Shimizu, Yumi ; Watanabe, Akira ; Kamei, Katsuhiko ; Shimizu, Kiminori</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3569-58fe02d9e952d506b6fcf82bceecf88eded457579d91a373af82657c90de266c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>3-Mercaptopyruvate sulfurtransferase</topic><topic>Amino acids</topic><topic>Antifungal agents</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biosynthesis</topic><topic>Cell Biology</topic><topic>Cryptococcus neoformans</topic><topic>Cysteine</topic><topic>Fungal infections</topic><topic>Fungi</topic><topic>Fungicides</topic><topic>Genes</topic><topic>Homology</topic><topic>Hydrogen sulfide</topic><topic>Life Sciences</topic><topic>Metabolic pathways</topic><topic>Methionine</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Original Article</topic><topic>Plant Sciences</topic><topic>Proteomics</topic><topic>Reductases</topic><topic>Sulfite</topic><topic>Sulfite reductase</topic><topic>Sulfur</topic><topic>Sulfurtransferase</topic><topic>Therapeutic targets</topic><topic>Virulence</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nguyen, Phuong-Thao</creatorcontrib><creatorcontrib>Toh-e, Akio</creatorcontrib><creatorcontrib>Nguyen, Ngoc-Hung</creatorcontrib><creatorcontrib>Imanishi-Shimizu, Yumi</creatorcontrib><creatorcontrib>Watanabe, Akira</creatorcontrib><creatorcontrib>Kamei, Katsuhiko</creatorcontrib><creatorcontrib>Shimizu, 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sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans</atitle><jtitle>Current genetics</jtitle><stitle>Curr Genet</stitle><addtitle>Curr Genet</addtitle><date>2021-02-01</date><risdate>2021</risdate><volume>67</volume><issue>1</issue><spage>115</spage><epage>128</epage><pages>115-128</pages><issn>0172-8083</issn><eissn>1432-0983</eissn><abstract>The amino acid biosynthetic pathway of invasive pathogenic fungi has been studied as a potential antifungal drug target. Studies of the disruption of genes involved in amino acid biosynthesis have demonstrated the importance of this pathway in the virulence of
Cryptococcus neoformans
. Here, we identified the
MET5
(
CNL05500
) and
MET10
(
CNG03990
) genes in this pathway, both encoding sulfite reductase, which catalyzes the reduction of sulfite to sulfide. The
MET14
(
CNE03880
) gene was also identified, which is responsible for the conversion of sulfate to sulfite. The use of cysteine as a sulfur source led to the production of methionine via hydrogen sulfide synthesis mediated by
CYS4
(
CNA06170
)
, CYS3
(
CNN01730
), and
MST1
(
CND03690
).
MST1
exhibited high homology with the
TUM1
gene of
Saccharomyces cerevisiae
, which has functional similarity with the 3-mercaptopyruvate sulfurtransferase (
3-MST
) gene in humans. Although the hypothesis that hydrogen sulfide is produced from cysteine via
CYS4
,
CYS3
, and
MST1
warrants further study, the new insight into the metabolic pathway of sulfur-containing amino acids in
C. neoformans
provided here indicates the usefulness of this system in the development of screening tools for antifungal drug agents.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>33001274</pmid><doi>10.1007/s00294-020-01112-9</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0001-5966-976X</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0172-8083 |
| ispartof | Current genetics, 2021-02, Vol.67 (1), p.115-128 |
| issn | 0172-8083 1432-0983 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2447841284 |
| source | Springer Nature - Complete Springer Journals |
| subjects | 3-Mercaptopyruvate sulfurtransferase Amino acids Antifungal agents Biochemistry Biomedical and Life Sciences Biosynthesis Cell Biology Cryptococcus neoformans Cysteine Fungal infections Fungi Fungicides Genes Homology Hydrogen sulfide Life Sciences Metabolic pathways Methionine Microbial Genetics and Genomics Microbiology Original Article Plant Sciences Proteomics Reductases Sulfite Sulfite reductase Sulfur Sulfurtransferase Therapeutic targets Virulence Yeasts |
| title | Identification and characterization of a sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans |
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