Reassessing the Potential Activities of Plant CGI-58 Protein
Comparative Gene Identification-58 (CGI-58) is a widespread protein found in animals and plants. This protein has been shown to participate in lipolysis in mice and humans by activating Adipose triglyceride lipase (ATGL), the initial enzyme responsible for the triacylglycerol (TAG) catabolism cascad...
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| creator | Khatib, Abdallah Arhab, Yani Bentebibel, Assia Abousalham, Abdelkarim Noiriel, Alexandre |
| description | Comparative Gene Identification-58 (CGI-58) is a widespread protein found in animals and plants. This protein has been shown to participate in lipolysis in mice and humans by activating Adipose triglyceride lipase (ATGL), the initial enzyme responsible for the triacylglycerol (TAG) catabolism cascade. Human mutation of CGI-58 is the cause of Chanarin-Dorfman syndrome, an orphan disease characterized by a systemic accumulation of TAG which engenders tissue disorders. The CGI-58 protein has also been shown to participate in neutral lipid metabolism in plants and, in this case, a mutation again provokes TAG accumulation. Although its roles as an ATGL coactivator and in lipid metabolism are quite clear, the catalytic activity of CGI-58 is still in question. The acyltransferase activities of CGI-58 have been speculated about, reported or even dismissed and experimental evidence that CGI-58 expressed in E. coli possesses an unambiguous catalytic activity is still lacking. To address this problem, we developed a new set of plasmids and site-directed mutants to elucidate the in vivo effects of CGI-58 expression on lipid metabolism in E. coli. By analyzing the lipid composition in selected E. coli strains expressing CGI-58 proteins, and by reinvestigating enzymatic tests with adequate controls, we show here that recombinant plant CGI-58 has none of the proposed activities previously described. Recombinant plant and mouse CGI-58 both lack acyltransferase activity towards either lysophosphatidylglycerol or lysophosphatidic acid to form phosphatidylglycerol or phosphatidic acid and recombinant plant CGI-58 does not catalyze TAG or phospholipid hydrolysis. However, expression of recombinant plant CGI-58, but not mouse CGI-58, led to a decrease in phosphatidylglycerol in all strains of E. coli tested, and a mutation of the putative catalytic residues restored a wild-type phenotype. The potential activities of plant CGI-58 are subsequently discussed. |
| doi_str_mv | 10.1371/journal.pone.0145806 |
| format | Article |
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This protein has been shown to participate in lipolysis in mice and humans by activating Adipose triglyceride lipase (ATGL), the initial enzyme responsible for the triacylglycerol (TAG) catabolism cascade. Human mutation of CGI-58 is the cause of Chanarin-Dorfman syndrome, an orphan disease characterized by a systemic accumulation of TAG which engenders tissue disorders. The CGI-58 protein has also been shown to participate in neutral lipid metabolism in plants and, in this case, a mutation again provokes TAG accumulation. Although its roles as an ATGL coactivator and in lipid metabolism are quite clear, the catalytic activity of CGI-58 is still in question. The acyltransferase activities of CGI-58 have been speculated about, reported or even dismissed and experimental evidence that CGI-58 expressed in E. coli possesses an unambiguous catalytic activity is still lacking. To address this problem, we developed a new set of plasmids and site-directed mutants to elucidate the in vivo effects of CGI-58 expression on lipid metabolism in E. coli. By analyzing the lipid composition in selected E. coli strains expressing CGI-58 proteins, and by reinvestigating enzymatic tests with adequate controls, we show here that recombinant plant CGI-58 has none of the proposed activities previously described. Recombinant plant and mouse CGI-58 both lack acyltransferase activity towards either lysophosphatidylglycerol or lysophosphatidic acid to form phosphatidylglycerol or phosphatidic acid and recombinant plant CGI-58 does not catalyze TAG or phospholipid hydrolysis. However, expression of recombinant plant CGI-58, but not mouse CGI-58, led to a decrease in phosphatidylglycerol in all strains of E. coli tested, and a mutation of the putative catalytic residues restored a wild-type phenotype. The potential activities of plant CGI-58 are subsequently discussed.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0145806</identifier><identifier>PMID: 26745266</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Accumulation ; Acids ; Acyltransferase ; Acyltransferases - chemistry ; Acyltransferases - genetics ; Acyltransferases - metabolism ; Amino Acid Sequence ; Animals ; Arabidopsis - enzymology ; Biocatalysis ; Biochemistry ; Biochemistry, Molecular Biology ; Catabolism ; Catalysis ; Catalytic activity ; Chemical properties ; Cloning, Molecular ; Copper ; E coli ; Electrophoresis, Polyacrylamide Gel ; Enzymes ; Escherichia coli ; Escherichia coli - metabolism ; Fatty acids ; Genetic aspects ; Health aspects ; Homeostasis ; Hydrolysis ; In vivo methods and tests ; Kinases ; Life Sciences ; Lipase ; Lipid composition ; Lipid Metabolism ; Lipids ; Lipolysis ; Lysophosphatidic acid ; Mammals ; Membranes ; Metabolism ; Mice ; Molecular biology ; Molecular Sequence Data ; Mutants ; Mutation ; Phenotype ; Phosphatidic acid ; Phosphatidylglycerol ; Phosphatidylglycerols - metabolism ; Phospholipids ; Plant proteins ; Plant Proteins - chemistry ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Plasmids ; Polyamines ; Proteins ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Sequence Alignment ; Sequence Homology, Amino Acid ; Triglycerides - metabolism</subject><ispartof>PloS one, 2016-01, Vol.11 (1), p.e0145806-e0145806</ispartof><rights>COPYRIGHT 2016 Public Library of Science</rights><rights>2016 Khatib et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>2016 Khatib et al 2016 Khatib et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c726t-5976208d3738795164890195a997f0775c71a523486403757f5f83411d1d33a63</citedby><cites>FETCH-LOGICAL-c726t-5976208d3738795164890195a997f0775c71a523486403757f5f83411d1d33a63</cites><orcidid>0000-0003-0979-1614</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4706320/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4706320/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,724,777,781,861,882,2096,2915,23847,27905,27906,53772,53774,79349,79350</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26745266$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01693107$$DView record in HAL$$Hfree_for_read</backlink></links><search><contributor>Oberer, Monika</contributor><creatorcontrib>Khatib, Abdallah</creatorcontrib><creatorcontrib>Arhab, Yani</creatorcontrib><creatorcontrib>Bentebibel, Assia</creatorcontrib><creatorcontrib>Abousalham, Abdelkarim</creatorcontrib><creatorcontrib>Noiriel, Alexandre</creatorcontrib><title>Reassessing the Potential Activities of Plant CGI-58 Protein</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Comparative Gene Identification-58 (CGI-58) is a widespread protein found in animals and plants. This protein has been shown to participate in lipolysis in mice and humans by activating Adipose triglyceride lipase (ATGL), the initial enzyme responsible for the triacylglycerol (TAG) catabolism cascade. Human mutation of CGI-58 is the cause of Chanarin-Dorfman syndrome, an orphan disease characterized by a systemic accumulation of TAG which engenders tissue disorders. The CGI-58 protein has also been shown to participate in neutral lipid metabolism in plants and, in this case, a mutation again provokes TAG accumulation. Although its roles as an ATGL coactivator and in lipid metabolism are quite clear, the catalytic activity of CGI-58 is still in question. The acyltransferase activities of CGI-58 have been speculated about, reported or even dismissed and experimental evidence that CGI-58 expressed in E. coli possesses an unambiguous catalytic activity is still lacking. To address this problem, we developed a new set of plasmids and site-directed mutants to elucidate the in vivo effects of CGI-58 expression on lipid metabolism in E. coli. By analyzing the lipid composition in selected E. coli strains expressing CGI-58 proteins, and by reinvestigating enzymatic tests with adequate controls, we show here that recombinant plant CGI-58 has none of the proposed activities previously described. Recombinant plant and mouse CGI-58 both lack acyltransferase activity towards either lysophosphatidylglycerol or lysophosphatidic acid to form phosphatidylglycerol or phosphatidic acid and recombinant plant CGI-58 does not catalyze TAG or phospholipid hydrolysis. However, expression of recombinant plant CGI-58, but not mouse CGI-58, led to a decrease in phosphatidylglycerol in all strains of E. coli tested, and a mutation of the putative catalytic residues restored a wild-type phenotype. The potential activities of plant CGI-58 are subsequently discussed.</description><subject>Accumulation</subject><subject>Acids</subject><subject>Acyltransferase</subject><subject>Acyltransferases - chemistry</subject><subject>Acyltransferases - genetics</subject><subject>Acyltransferases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Arabidopsis - enzymology</subject><subject>Biocatalysis</subject><subject>Biochemistry</subject><subject>Biochemistry, Molecular Biology</subject><subject>Catabolism</subject><subject>Catalysis</subject><subject>Catalytic activity</subject><subject>Chemical properties</subject><subject>Cloning, Molecular</subject><subject>Copper</subject><subject>E coli</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Fatty acids</subject><subject>Genetic aspects</subject><subject>Health aspects</subject><subject>Homeostasis</subject><subject>Hydrolysis</subject><subject>In vivo methods and tests</subject><subject>Kinases</subject><subject>Life Sciences</subject><subject>Lipase</subject><subject>Lipid composition</subject><subject>Lipid Metabolism</subject><subject>Lipids</subject><subject>Lipolysis</subject><subject>Lysophosphatidic acid</subject><subject>Mammals</subject><subject>Membranes</subject><subject>Metabolism</subject><subject>Mice</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Phenotype</subject><subject>Phosphatidic acid</subject><subject>Phosphatidylglycerol</subject><subject>Phosphatidylglycerols - metabolism</subject><subject>Phospholipids</subject><subject>Plant proteins</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Plasmids</subject><subject>Polyamines</subject><subject>Proteins</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Triglycerides - metabolism</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</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><sourceid>DOA</sourceid><recordid>eNqNk11r2zAUhs3YWLts_2BshsFYL5xJ1jeMQQhbGwg0dB-3QpFlR8GxMksO7b-fvLglLr0YvrA5ft736Lz2SZK3EEwhYvDz1nVto-rp3jVmCiAmHNBnyTkUKM9oDtDzk-ez5JX3WwAI4pS-TM5yyjDJKT1PvtwY5b3x3jZVGjYmXblgmmBVnc50sAcbrPGpK9NVrZqQzi8XGeHpqo2UbV4nL0pVe_NmuE-SX9-__ZxfZcvry8V8tsw0y2nIiGDxELxADHEmCKSYCwAFUUKwEjBGNIOK5AhzigFihJWk5AhDWMACIUXRJHl_9N3XzsthcC8hIwRQgiCPxOJIFE5t5b61O9XeSaes_FdwbSVVG6yujYRFKThhkBc4xxyDtdaarYESoMyVwDB6fR26deudKXSMo1X1yHT8prEbWbmDxAxQFNOeJBdHg80j2dVsKfsagFQgCNihb_ZpaNa6P53xQe6s16aOaRvX9TNSwAkVorf98Ah9OomBqlQc1jali2fUvamcYSQQwjHwSE2foOJVmJ3V8Y8qbayPBBcjQWSCuQ2V6ryXix83_89e_x6zH0_YjVF12HhXd8G6xo9BfAR167xvTfmQLASyX4j7NGS_EHJYiCh7d_oxH0T3G4D-Aktn_3c</recordid><startdate>20160108</startdate><enddate>20160108</enddate><creator>Khatib, Abdallah</creator><creator>Arhab, Yani</creator><creator>Bentebibel, Assia</creator><creator>Abousalham, Abdelkarim</creator><creator>Noiriel, Alexandre</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</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>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0003-0979-1614</orcidid></search><sort><creationdate>20160108</creationdate><title>Reassessing the Potential Activities of Plant CGI-58 Protein</title><author>Khatib, Abdallah ; Arhab, Yani ; Bentebibel, Assia ; Abousalham, Abdelkarim ; Noiriel, Alexandre</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c726t-5976208d3738795164890195a997f0775c71a523486403757f5f83411d1d33a63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Accumulation</topic><topic>Acids</topic><topic>Acyltransferase</topic><topic>Acyltransferases - chemistry</topic><topic>Acyltransferases - genetics</topic><topic>Acyltransferases - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Arabidopsis - enzymology</topic><topic>Biocatalysis</topic><topic>Biochemistry</topic><topic>Biochemistry, Molecular Biology</topic><topic>Catabolism</topic><topic>Catalysis</topic><topic>Catalytic activity</topic><topic>Chemical properties</topic><topic>Cloning, Molecular</topic><topic>Copper</topic><topic>E coli</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - metabolism</topic><topic>Fatty acids</topic><topic>Genetic aspects</topic><topic>Health aspects</topic><topic>Homeostasis</topic><topic>Hydrolysis</topic><topic>In vivo methods and tests</topic><topic>Kinases</topic><topic>Life Sciences</topic><topic>Lipase</topic><topic>Lipid composition</topic><topic>Lipid Metabolism</topic><topic>Lipids</topic><topic>Lipolysis</topic><topic>Lysophosphatidic acid</topic><topic>Mammals</topic><topic>Membranes</topic><topic>Metabolism</topic><topic>Mice</topic><topic>Molecular biology</topic><topic>Molecular Sequence Data</topic><topic>Mutants</topic><topic>Mutation</topic><topic>Phenotype</topic><topic>Phosphatidic acid</topic><topic>Phosphatidylglycerol</topic><topic>Phosphatidylglycerols - 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Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Khatib, Abdallah</au><au>Arhab, Yani</au><au>Bentebibel, Assia</au><au>Abousalham, Abdelkarim</au><au>Noiriel, Alexandre</au><au>Oberer, Monika</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reassessing the Potential Activities of Plant CGI-58 Protein</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2016-01-08</date><risdate>2016</risdate><volume>11</volume><issue>1</issue><spage>e0145806</spage><epage>e0145806</epage><pages>e0145806-e0145806</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Comparative Gene Identification-58 (CGI-58) is a widespread protein found in animals and plants. This protein has been shown to participate in lipolysis in mice and humans by activating Adipose triglyceride lipase (ATGL), the initial enzyme responsible for the triacylglycerol (TAG) catabolism cascade. Human mutation of CGI-58 is the cause of Chanarin-Dorfman syndrome, an orphan disease characterized by a systemic accumulation of TAG which engenders tissue disorders. The CGI-58 protein has also been shown to participate in neutral lipid metabolism in plants and, in this case, a mutation again provokes TAG accumulation. Although its roles as an ATGL coactivator and in lipid metabolism are quite clear, the catalytic activity of CGI-58 is still in question. The acyltransferase activities of CGI-58 have been speculated about, reported or even dismissed and experimental evidence that CGI-58 expressed in E. coli possesses an unambiguous catalytic activity is still lacking. To address this problem, we developed a new set of plasmids and site-directed mutants to elucidate the in vivo effects of CGI-58 expression on lipid metabolism in E. coli. By analyzing the lipid composition in selected E. coli strains expressing CGI-58 proteins, and by reinvestigating enzymatic tests with adequate controls, we show here that recombinant plant CGI-58 has none of the proposed activities previously described. Recombinant plant and mouse CGI-58 both lack acyltransferase activity towards either lysophosphatidylglycerol or lysophosphatidic acid to form phosphatidylglycerol or phosphatidic acid and recombinant plant CGI-58 does not catalyze TAG or phospholipid hydrolysis. However, expression of recombinant plant CGI-58, but not mouse CGI-58, led to a decrease in phosphatidylglycerol in all strains of E. coli tested, and a mutation of the putative catalytic residues restored a wild-type phenotype. The potential activities of plant CGI-58 are subsequently discussed.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>26745266</pmid><doi>10.1371/journal.pone.0145806</doi><orcidid>https://orcid.org/0000-0003-0979-1614</orcidid><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2016-01, Vol.11 (1), p.e0145806-e0145806 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1755065318 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Public Library of Science (PLoS); PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Accumulation Acids Acyltransferase Acyltransferases - chemistry Acyltransferases - genetics Acyltransferases - metabolism Amino Acid Sequence Animals Arabidopsis - enzymology Biocatalysis Biochemistry Biochemistry, Molecular Biology Catabolism Catalysis Catalytic activity Chemical properties Cloning, Molecular Copper E coli Electrophoresis, Polyacrylamide Gel Enzymes Escherichia coli Escherichia coli - metabolism Fatty acids Genetic aspects Health aspects Homeostasis Hydrolysis In vivo methods and tests Kinases Life Sciences Lipase Lipid composition Lipid Metabolism Lipids Lipolysis Lysophosphatidic acid Mammals Membranes Metabolism Mice Molecular biology Molecular Sequence Data Mutants Mutation Phenotype Phosphatidic acid Phosphatidylglycerol Phosphatidylglycerols - metabolism Phospholipids Plant proteins Plant Proteins - chemistry Plant Proteins - genetics Plant Proteins - metabolism Plasmids Polyamines Proteins Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Sequence Alignment Sequence Homology, Amino Acid Triglycerides - metabolism |
| title | Reassessing the Potential Activities of Plant CGI-58 Protein |
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