Role of Saccharomyces cerevisiae serine O-acetyltransferase in cysteine biosynthesis
Some strains of Saccharomyces cerevisiae have detectable activities of L-serine O-acetyltransferase (SATase) and O-acetyl-L-serine/O-acetyl-L-homoserine sulfhydrylase (OAS/OAH-SHLase), but synthesize L-cysteine exclusively via cystathionine by cystathionine beta-synthase and cystathionine gamma-lyas...
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Veröffentlicht in: | FEMS microbiology letters 2003-01, Vol.218 (2), p.291-297 |
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creator | Takagi, H Yoshioka, K Awano, N Nakamori, S Ono, B.I |
description | Some strains of Saccharomyces cerevisiae have detectable activities of L-serine O-acetyltransferase (SATase) and O-acetyl-L-serine/O-acetyl-L-homoserine sulfhydrylase (OAS/OAH-SHLase), but synthesize L-cysteine exclusively via cystathionine by cystathionine beta-synthase and cystathionine gamma-lyase. To untangle this peculiar feature in sulfur metabolism, we introduced Escherichia coli genes encoding SATase and OAS-SHLase into S. cerevisiae L-cysteine auxotrophs. While the cells expressing SATase grew on medium lacking L-cysteine, those expressing OAS-SHLase did not grow at all. The cells expressing both enzymes grew very well without L-cysteine. These results indicate that S. cerevisiae SATase cannot support L-cysteine biosynthesis and that S. cerevisiae OAS/OAH-SHLase produces L-cysteine if enough OAS is provided by E. coli SATase. It appears as if S. cerevisiae SATase does not possess a metabolic role in vivo either because of very low activity or localization. For example, S. cerevisiae SATase may be localized in the nucleus, thus controlling the level of OAS required for regulation of sulfate assimilation, but playing no role in the direct synthesis of L-cysteine. |
doi_str_mv | 10.1111/j.1574-6968.2003.tb11531.x |
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To untangle this peculiar feature in sulfur metabolism, we introduced Escherichia coli genes encoding SATase and OAS-SHLase into S. cerevisiae L-cysteine auxotrophs. While the cells expressing SATase grew on medium lacking L-cysteine, those expressing OAS-SHLase did not grow at all. The cells expressing both enzymes grew very well without L-cysteine. These results indicate that S. cerevisiae SATase cannot support L-cysteine biosynthesis and that S. cerevisiae OAS/OAH-SHLase produces L-cysteine if enough OAS is provided by E. coli SATase. It appears as if S. cerevisiae SATase does not possess a metabolic role in vivo either because of very low activity or localization. For example, S. cerevisiae SATase may be localized in the nucleus, thus controlling the level of OAS required for regulation of sulfate assimilation, but playing no role in the direct synthesis of L-cysteine.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2003.tb11531.x</identifier><identifier>PMID: 12586406</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Acetyltransferase ; Acetyltransferases - antagonists & inhibitors ; Acetyltransferases - physiology ; Auxotrophs ; Biological and medical sciences ; Biosynthesis ; Carbon-Oxygen Lyases - metabolism ; cystathionine ; cystathionine beta-synthase ; cystathionine gamma-lyase ; Cysteine ; Cysteine - biosynthesis ; Cysteine Synthase ; E coli ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; genes ; Growth, nutrition, metabolism, transports, enzymes. Molecular biology ; L-Serine ; Localization ; Lyases - metabolism ; l‐Cysteine biosynthesis ; l‐Serine O‐acetyltransferase ; Microbiology ; Multienzyme Complexes ; Mycology ; O‐Acetyl‐l‐serine sulfhydrylase ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins ; Serine O-Acetyltransferase ; Sulfates ; Sulfates - metabolism ; Sulfhydrylase ; Sulfur ; Yeast</subject><ispartof>FEMS microbiology letters, 2003-01, Vol.218 (2), p.291-297</ispartof><rights>2002 Federation of European Microbiological Societies 2002</rights><rights>2003 INIST-CNRS</rights><rights>2002 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4611-1d2393a858b62ba45527e5a0b83d3837f1dc60b99d7437c1444905f2589bf263</citedby><cites>FETCH-LOGICAL-c4611-1d2393a858b62ba45527e5a0b83d3837f1dc60b99d7437c1444905f2589bf263</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.2003.tb11531.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2003.tb11531.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27922,27923,45572,45573</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14486784$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12586406$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Takagi, H</creatorcontrib><creatorcontrib>Yoshioka, K</creatorcontrib><creatorcontrib>Awano, N</creatorcontrib><creatorcontrib>Nakamori, S</creatorcontrib><creatorcontrib>Ono, B.I</creatorcontrib><title>Role of Saccharomyces cerevisiae serine O-acetyltransferase in cysteine biosynthesis</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Some strains of Saccharomyces cerevisiae have detectable activities of L-serine O-acetyltransferase (SATase) and O-acetyl-L-serine/O-acetyl-L-homoserine sulfhydrylase (OAS/OAH-SHLase), but synthesize L-cysteine exclusively via cystathionine by cystathionine beta-synthase and cystathionine gamma-lyase. To untangle this peculiar feature in sulfur metabolism, we introduced Escherichia coli genes encoding SATase and OAS-SHLase into S. cerevisiae L-cysteine auxotrophs. While the cells expressing SATase grew on medium lacking L-cysteine, those expressing OAS-SHLase did not grow at all. The cells expressing both enzymes grew very well without L-cysteine. These results indicate that S. cerevisiae SATase cannot support L-cysteine biosynthesis and that S. cerevisiae OAS/OAH-SHLase produces L-cysteine if enough OAS is provided by E. coli SATase. It appears as if S. cerevisiae SATase does not possess a metabolic role in vivo either because of very low activity or localization. For example, S. cerevisiae SATase may be localized in the nucleus, thus controlling the level of OAS required for regulation of sulfate assimilation, but playing no role in the direct synthesis of L-cysteine.</description><subject>Acetyltransferase</subject><subject>Acetyltransferases - antagonists & inhibitors</subject><subject>Acetyltransferases - physiology</subject><subject>Auxotrophs</subject><subject>Biological and medical sciences</subject><subject>Biosynthesis</subject><subject>Carbon-Oxygen Lyases - metabolism</subject><subject>cystathionine</subject><subject>cystathionine beta-synthase</subject><subject>cystathionine gamma-lyase</subject><subject>Cysteine</subject><subject>Cysteine - biosynthesis</subject><subject>Cysteine Synthase</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Growth, nutrition, metabolism, transports, enzymes. Molecular biology</subject><subject>L-Serine</subject><subject>Localization</subject><subject>Lyases - metabolism</subject><subject>l‐Cysteine biosynthesis</subject><subject>l‐Serine O‐acetyltransferase</subject><subject>Microbiology</subject><subject>Multienzyme Complexes</subject><subject>Mycology</subject><subject>O‐Acetyl‐l‐serine sulfhydrylase</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Serine O-Acetyltransferase</subject><subject>Sulfates</subject><subject>Sulfates - metabolism</subject><subject>Sulfhydrylase</subject><subject>Sulfur</subject><subject>Yeast</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqVkV-L1DAUxYMo7rj6FbQo-taam__1QVgWV4WRBXd8Dmmauhk67WzSuttvb0qLC6KIecnD_Z2bc3IQegm4gHTe7gvgkuWiFKogGNNiqAA4heLuAdr8Gj1EG0ylygGX8gQ9iXGPMWYEi8foBAhXgmGxQbuvfeuyvsmujLXXJvSHybqYWRfcDx-9cVl0wXcuu8yNdcPUDsF0sXHBRJf5LrNTHNw8r3wfp264dtHHp-hRY9ronq33KdpdfNidf8q3lx8_n59tc8sEQA41oSU1iqtKkMowzol03OBK0ZoqKhuorcBVWdaSUWmBMVZi3iTvZdUQQU_Rm2XtMfQ3o4uDPvhoXduazvVj1JJiQkGpf4KghFREQAJf_Qbu-zF0KYMmFEuQXBCaqHcLZUMfY3CNPgZ_MGHSgPXckN7ruQY916DnhvTakL5L4ufrE2N1cPW9dK0kAa9XwERr2ib9t_XxnmNsdssS937hbn3rpv-woC--bEk5h-XLgn48_kWe_znBi0XXmF6b7yGZ-3ZFMAiMAZRUgv4E54TFSw</recordid><startdate>200301</startdate><enddate>200301</enddate><creator>Takagi, H</creator><creator>Yoshioka, K</creator><creator>Awano, N</creator><creator>Nakamori, S</creator><creator>Ono, B.I</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</general><scope>FBQ</scope><scope>IQODW</scope><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>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</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>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>H94</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>RC3</scope><scope>7X8</scope></search><sort><creationdate>200301</creationdate><title>Role of Saccharomyces cerevisiae serine O-acetyltransferase in cysteine biosynthesis</title><author>Takagi, H ; Yoshioka, K ; Awano, N ; Nakamori, S ; Ono, B.I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4611-1d2393a858b62ba45527e5a0b83d3837f1dc60b99d7437c1444905f2589bf263</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Acetyltransferase</topic><topic>Acetyltransferases - antagonists & inhibitors</topic><topic>Acetyltransferases - physiology</topic><topic>Auxotrophs</topic><topic>Biological and medical sciences</topic><topic>Biosynthesis</topic><topic>Carbon-Oxygen Lyases - metabolism</topic><topic>cystathionine</topic><topic>cystathionine beta-synthase</topic><topic>cystathionine gamma-lyase</topic><topic>Cysteine</topic><topic>Cysteine - biosynthesis</topic><topic>Cysteine Synthase</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Growth, nutrition, metabolism, transports, enzymes. Molecular biology</topic><topic>L-Serine</topic><topic>Localization</topic><topic>Lyases - metabolism</topic><topic>l‐Cysteine biosynthesis</topic><topic>l‐Serine O‐acetyltransferase</topic><topic>Microbiology</topic><topic>Multienzyme Complexes</topic><topic>Mycology</topic><topic>O‐Acetyl‐l‐serine sulfhydrylase</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Serine O-Acetyltransferase</topic><topic>Sulfates</topic><topic>Sulfates - metabolism</topic><topic>Sulfhydrylase</topic><topic>Sulfur</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Takagi, H</creatorcontrib><creatorcontrib>Yoshioka, K</creatorcontrib><creatorcontrib>Awano, N</creatorcontrib><creatorcontrib>Nakamori, S</creatorcontrib><creatorcontrib>Ono, B.I</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><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>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>ProQuest Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest Public Health Database</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 One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</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>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</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>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Takagi, H</au><au>Yoshioka, K</au><au>Awano, N</au><au>Nakamori, S</au><au>Ono, B.I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of Saccharomyces cerevisiae serine O-acetyltransferase in cysteine biosynthesis</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2003-01</date><risdate>2003</risdate><volume>218</volume><issue>2</issue><spage>291</spage><epage>297</epage><pages>291-297</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Some strains of Saccharomyces cerevisiae have detectable activities of L-serine O-acetyltransferase (SATase) and O-acetyl-L-serine/O-acetyl-L-homoserine sulfhydrylase (OAS/OAH-SHLase), but synthesize L-cysteine exclusively via cystathionine by cystathionine beta-synthase and cystathionine gamma-lyase. To untangle this peculiar feature in sulfur metabolism, we introduced Escherichia coli genes encoding SATase and OAS-SHLase into S. cerevisiae L-cysteine auxotrophs. While the cells expressing SATase grew on medium lacking L-cysteine, those expressing OAS-SHLase did not grow at all. The cells expressing both enzymes grew very well without L-cysteine. These results indicate that S. cerevisiae SATase cannot support L-cysteine biosynthesis and that S. cerevisiae OAS/OAH-SHLase produces L-cysteine if enough OAS is provided by E. coli SATase. It appears as if S. cerevisiae SATase does not possess a metabolic role in vivo either because of very low activity or localization. For example, S. cerevisiae SATase may be localized in the nucleus, thus controlling the level of OAS required for regulation of sulfate assimilation, but playing no role in the direct synthesis of L-cysteine.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>12586406</pmid><doi>10.1111/j.1574-6968.2003.tb11531.x</doi><tpages>7</tpages></addata></record> |
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subjects | Acetyltransferase Acetyltransferases - antagonists & inhibitors Acetyltransferases - physiology Auxotrophs Biological and medical sciences Biosynthesis Carbon-Oxygen Lyases - metabolism cystathionine cystathionine beta-synthase cystathionine gamma-lyase Cysteine Cysteine - biosynthesis Cysteine Synthase E coli Escherichia coli Fundamental and applied biological sciences. Psychology genes Growth, nutrition, metabolism, transports, enzymes. Molecular biology L-Serine Localization Lyases - metabolism l‐Cysteine biosynthesis l‐Serine O‐acetyltransferase Microbiology Multienzyme Complexes Mycology O‐Acetyl‐l‐serine sulfhydrylase Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Serine O-Acetyltransferase Sulfates Sulfates - metabolism Sulfhydrylase Sulfur Yeast |
title | Role of Saccharomyces cerevisiae serine O-acetyltransferase in cysteine biosynthesis |
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