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The YIG1 (YPL201c) encoded protein is involved in regulating anaerobic glycerol metabolism in Saccharomyces cerevisiae
Under anaerobic conditions S. cerevisiae produces glycerol to regenerate NAD+ from the excess NADH produced in cell metabolism. We here report on the role of an uncharacterized protein, Yig1p (Ypl201cp), in anaerobic glycerol production. Yig1p was previously shown to interact in two‐hybrid tests wit...
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Published in: | Yeast (Chichester, England) England), 2005-12, Vol.22 (16), p.1257-1268 |
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creator | Granath, K. Modig, T. Forsmark, A. Adler, L. Lidén, G. |
description | Under anaerobic conditions S. cerevisiae produces glycerol to regenerate NAD+ from the excess NADH produced in cell metabolism. We here report on the role of an uncharacterized protein, Yig1p (Ypl201cp), in anaerobic glycerol production. Yig1p was previously shown to interact in two‐hybrid tests with the GPP1 and GPP2 encoded glycerol 3‐phosphatase (Gpp), and we here demonstrate that strains overexpressing YIG1 show strongly decreased Gpp activity and content of the major phosphatase, Gpp1p. However, cells overexpressing YIG1 exhibited only slightly decreased GPP1 transcript levels, suggesting that Yig1p modulates expression on both transcriptional and post‐transcriptional levels. In agreement with such a role, a GFP‐tagged derivate of Yig1p was localized to both the cytosol and the nucleus. Deletion or overexpression of YIG1 did not, however, significantly affect growth yield or glycerol yield in anaerobic batch cultures, which is consistent with the previously proposed low flux control exerted at the Gpp level. Copyright © 2005 John Wiley & Sons, Ltd. |
doi_str_mv | 10.1002/yea.1307 |
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We here report on the role of an uncharacterized protein, Yig1p (Ypl201cp), in anaerobic glycerol production. Yig1p was previously shown to interact in two‐hybrid tests with the GPP1 and GPP2 encoded glycerol 3‐phosphatase (Gpp), and we here demonstrate that strains overexpressing YIG1 show strongly decreased Gpp activity and content of the major phosphatase, Gpp1p. However, cells overexpressing YIG1 exhibited only slightly decreased GPP1 transcript levels, suggesting that Yig1p modulates expression on both transcriptional and post‐transcriptional levels. In agreement with such a role, a GFP‐tagged derivate of Yig1p was localized to both the cytosol and the nucleus. Deletion or overexpression of YIG1 did not, however, significantly affect growth yield or glycerol yield in anaerobic batch cultures, which is consistent with the previously proposed low flux control exerted at the Gpp level. Copyright © 2005 John Wiley & Sons, Ltd.</description><identifier>ISSN: 0749-503X</identifier><identifier>EISSN: 1097-0061</identifier><identifier>DOI: 10.1002/yea.1307</identifier><identifier>PMID: 16358322</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Anaerobiosis ; Blotting, Northern ; Blotting, Western ; DNA, Fungal - genetics ; DNA, Fungal - metabolism ; Gene Expression ; glycerol ; Glycerol - metabolism ; Glycerolphosphate Dehydrogenase - biosynthesis ; Glycerolphosphate Dehydrogenase - genetics ; Glycerolphosphate Dehydrogenase - metabolism ; GPP1 ; Oxidation-Reduction ; phosphatase ; Phosphoric Monoester Hydrolases - biosynthesis ; Phosphoric Monoester Hydrolases - genetics ; Phosphoric Monoester Hydrolases - metabolism ; Polymerase Chain Reaction ; RNA, Messenger - biosynthesis ; RNA, Messenger - genetics ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism</subject><ispartof>Yeast (Chichester, England), 2005-12, Vol.22 (16), p.1257-1268</ispartof><rights>Copyright © 2005 John Wiley & Sons, Ltd.</rights><rights>Copyright 2005 John Wiley & Sons, Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2657-f45028b87464af9e829f366825fe1b03362024a6adf2059162693e32ac36d50d3</citedby><cites>FETCH-LOGICAL-c2657-f45028b87464af9e829f366825fe1b03362024a6adf2059162693e32ac36d50d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16358322$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Granath, K.</creatorcontrib><creatorcontrib>Modig, T.</creatorcontrib><creatorcontrib>Forsmark, A.</creatorcontrib><creatorcontrib>Adler, L.</creatorcontrib><creatorcontrib>Lidén, G.</creatorcontrib><title>The YIG1 (YPL201c) encoded protein is involved in regulating anaerobic glycerol metabolism in Saccharomyces cerevisiae</title><title>Yeast (Chichester, England)</title><addtitle>Yeast</addtitle><description>Under anaerobic conditions S. cerevisiae produces glycerol to regenerate NAD+ from the excess NADH produced in cell metabolism. We here report on the role of an uncharacterized protein, Yig1p (Ypl201cp), in anaerobic glycerol production. Yig1p was previously shown to interact in two‐hybrid tests with the GPP1 and GPP2 encoded glycerol 3‐phosphatase (Gpp), and we here demonstrate that strains overexpressing YIG1 show strongly decreased Gpp activity and content of the major phosphatase, Gpp1p. However, cells overexpressing YIG1 exhibited only slightly decreased GPP1 transcript levels, suggesting that Yig1p modulates expression on both transcriptional and post‐transcriptional levels. In agreement with such a role, a GFP‐tagged derivate of Yig1p was localized to both the cytosol and the nucleus. Deletion or overexpression of YIG1 did not, however, significantly affect growth yield or glycerol yield in anaerobic batch cultures, which is consistent with the previously proposed low flux control exerted at the Gpp level. Copyright © 2005 John Wiley & Sons, Ltd.</description><subject>Anaerobiosis</subject><subject>Blotting, Northern</subject><subject>Blotting, Western</subject><subject>DNA, Fungal - genetics</subject><subject>DNA, Fungal - metabolism</subject><subject>Gene Expression</subject><subject>glycerol</subject><subject>Glycerol - metabolism</subject><subject>Glycerolphosphate Dehydrogenase - biosynthesis</subject><subject>Glycerolphosphate Dehydrogenase - genetics</subject><subject>Glycerolphosphate Dehydrogenase - metabolism</subject><subject>GPP1</subject><subject>Oxidation-Reduction</subject><subject>phosphatase</subject><subject>Phosphoric Monoester Hydrolases - biosynthesis</subject><subject>Phosphoric Monoester Hydrolases - genetics</subject><subject>Phosphoric Monoester Hydrolases - metabolism</subject><subject>Polymerase Chain Reaction</subject><subject>RNA, Messenger - biosynthesis</subject><subject>RNA, Messenger - genetics</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><issn>0749-503X</issn><issn>1097-0061</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqF0V1LwzAUBuAgis4p-AskVzIvOk-SJm0vZcwPGCg4wV2VND2dkbSdzTbZvzdzA6_Eq3w9vHDyEnLBYMgA-M0G9ZAJSA5Ij0GWRACKHZIeJHEWSRBvJ-TU-w8AxiRPj8kJU0KmgvMeWU_fkc4e7xkdzJ4nHJi5ptiYtsSSLrp2ibah1lPbrFu3Dnfh2OF85fTSNnOqG41dW1hD525jwtbRGpe6aJ319da-aGPeddfW4dXTIHBtvdV4Ro4q7Tye79c-eb0bT0cP0eTp_nF0O4kMVzKJqlgCT4s0iVWsqwxTnlVCqZTLClkBQigOPNZKlxUHmTHFVSZQcG2EKiWUok-udrlhls8V-mVeW2_QOd1gu_K5SjMWZzz5F3JQiQTJAhzsoOla7zus8kVna91tcgb5tow8lJFvywj0cp-5Kmosf-H-9wOIduDLOtz8GZTPxrc_gd_6wZHM</recordid><startdate>200512</startdate><enddate>200512</enddate><creator>Granath, K.</creator><creator>Modig, T.</creator><creator>Forsmark, A.</creator><creator>Adler, L.</creator><creator>Lidén, G.</creator><general>John Wiley & Sons, Ltd</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>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200512</creationdate><title>The YIG1 (YPL201c) encoded protein is involved in regulating anaerobic glycerol metabolism in Saccharomyces cerevisiae</title><author>Granath, K. ; Modig, T. ; Forsmark, A. ; Adler, L. ; Lidén, G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2657-f45028b87464af9e829f366825fe1b03362024a6adf2059162693e32ac36d50d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Anaerobiosis</topic><topic>Blotting, Northern</topic><topic>Blotting, Western</topic><topic>DNA, Fungal - genetics</topic><topic>DNA, Fungal - metabolism</topic><topic>Gene Expression</topic><topic>glycerol</topic><topic>Glycerol - metabolism</topic><topic>Glycerolphosphate Dehydrogenase - biosynthesis</topic><topic>Glycerolphosphate Dehydrogenase - genetics</topic><topic>Glycerolphosphate Dehydrogenase - metabolism</topic><topic>GPP1</topic><topic>Oxidation-Reduction</topic><topic>phosphatase</topic><topic>Phosphoric Monoester Hydrolases - biosynthesis</topic><topic>Phosphoric Monoester Hydrolases - genetics</topic><topic>Phosphoric Monoester Hydrolases - metabolism</topic><topic>Polymerase Chain Reaction</topic><topic>RNA, Messenger - biosynthesis</topic><topic>RNA, Messenger - genetics</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Granath, K.</creatorcontrib><creatorcontrib>Modig, T.</creatorcontrib><creatorcontrib>Forsmark, A.</creatorcontrib><creatorcontrib>Adler, L.</creatorcontrib><creatorcontrib>Lidén, G.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</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>Yeast (Chichester, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Granath, K.</au><au>Modig, T.</au><au>Forsmark, A.</au><au>Adler, L.</au><au>Lidén, G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The YIG1 (YPL201c) encoded protein is involved in regulating anaerobic glycerol metabolism in Saccharomyces cerevisiae</atitle><jtitle>Yeast (Chichester, England)</jtitle><addtitle>Yeast</addtitle><date>2005-12</date><risdate>2005</risdate><volume>22</volume><issue>16</issue><spage>1257</spage><epage>1268</epage><pages>1257-1268</pages><issn>0749-503X</issn><eissn>1097-0061</eissn><abstract>Under anaerobic conditions S. cerevisiae produces glycerol to regenerate NAD+ from the excess NADH produced in cell metabolism. We here report on the role of an uncharacterized protein, Yig1p (Ypl201cp), in anaerobic glycerol production. Yig1p was previously shown to interact in two‐hybrid tests with the GPP1 and GPP2 encoded glycerol 3‐phosphatase (Gpp), and we here demonstrate that strains overexpressing YIG1 show strongly decreased Gpp activity and content of the major phosphatase, Gpp1p. However, cells overexpressing YIG1 exhibited only slightly decreased GPP1 transcript levels, suggesting that Yig1p modulates expression on both transcriptional and post‐transcriptional levels. In agreement with such a role, a GFP‐tagged derivate of Yig1p was localized to both the cytosol and the nucleus. Deletion or overexpression of YIG1 did not, however, significantly affect growth yield or glycerol yield in anaerobic batch cultures, which is consistent with the previously proposed low flux control exerted at the Gpp level. Copyright © 2005 John Wiley & Sons, Ltd.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>16358322</pmid><doi>10.1002/yea.1307</doi><tpages>12</tpages></addata></record> |
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subjects | Anaerobiosis Blotting, Northern Blotting, Western DNA, Fungal - genetics DNA, Fungal - metabolism Gene Expression glycerol Glycerol - metabolism Glycerolphosphate Dehydrogenase - biosynthesis Glycerolphosphate Dehydrogenase - genetics Glycerolphosphate Dehydrogenase - metabolism GPP1 Oxidation-Reduction phosphatase Phosphoric Monoester Hydrolases - biosynthesis Phosphoric Monoester Hydrolases - genetics Phosphoric Monoester Hydrolases - metabolism Polymerase Chain Reaction RNA, Messenger - biosynthesis RNA, Messenger - genetics Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism |
title | The YIG1 (YPL201c) encoded protein is involved in regulating anaerobic glycerol metabolism in Saccharomyces cerevisiae |
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