Distribution of Macromolecular Methylations in Promastigotes of Leishmania donovani and Impact of Sinefungin
Sinefungin, an antifungal and antiparasitic nucleoside antibiotic, is a very potent antileishmanial agent both in vitro and in vivo. This molecule, structurally related to S‐adenosylmethionine, is a good competitive inhibitor of methyltransferases in vitro. The aim of this report is to analyze the i...
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| Veröffentlicht in: | The Journal of eukaryotic microbiology 1993-09, Vol.40 (5), p.581-589 |
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| container_title | The Journal of eukaryotic microbiology |
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| creator | LAWRENCE, FRANÇOISE ROBERT-GERO, MALKA |
| description | Sinefungin, an antifungal and antiparasitic nucleoside antibiotic, is a very potent antileishmanial agent both in vitro and in vivo. This molecule, structurally related to S‐adenosylmethionine, is a good competitive inhibitor of methyltransferases in vitro. The aim of this report is to analyze the impact of sinefungin on methylation pattern and the subcellular localisation of methyl groups and various methylases in promastigotes of Leishmania donovani. We have shown the presence of various methylated macromolecules in different subcellular fractions, with somewhat higher concentration in membrane fraction. In vitro, sinefungin inhibits the three main protein methylases, but in cells cultured in its presence the protein carboxylmethylations are specifically inhibited. |
| doi_str_mv | 10.1111/j.1550-7408.1993.tb06111.x |
| format | Article |
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This molecule, structurally related to S‐adenosylmethionine, is a good competitive inhibitor of methyltransferases in vitro. The aim of this report is to analyze the impact of sinefungin on methylation pattern and the subcellular localisation of methyl groups and various methylases in promastigotes of Leishmania donovani. We have shown the presence of various methylated macromolecules in different subcellular fractions, with somewhat higher concentration in membrane fraction. In vitro, sinefungin inhibits the three main protein methylases, but in cells cultured in its presence the protein carboxylmethylations are specifically inhibited.</description><identifier>ISSN: 1066-5234</identifier><identifier>EISSN: 1550-7408</identifier><identifier>DOI: 10.1111/j.1550-7408.1993.tb06111.x</identifier><identifier>PMID: 8401471</identifier><identifier>CODEN: JEMIED</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Adenosine - analogs & derivatives ; Adenosine - pharmacology ; Animals ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; Antiparasitic agents ; Biological and medical sciences ; Carboxylmethylation ; cell fractionation ; hemoflagellate ; Leishmania donovani ; Leishmania donovani - drug effects ; Leishmania donovani - growth & development ; Leishmania donovani - metabolism ; Macromolecular Substances ; Medical sciences ; methylated amino acids ; Methylation ; Pharmacology. Drug treatments ; protein methyltransferases ; Protein Methyltransferases - antagonists & inhibitors ; Protein Methyltransferases - metabolism ; Protozoa ; Protozoan Proteins - metabolism ; S-adenosylmethionine ; S-Adenosylmethionine - biosynthesis ; S-Adenosylmethionine - metabolism ; subcellular distribution of methyl groups ; Subcellular Fractions - metabolism</subject><ispartof>The Journal of eukaryotic microbiology, 1993-09, Vol.40 (5), p.581-589</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4671-10bbf6ecafbe2a6b761e7cc947b09010697abee4ba99697472ae9dd871a3fd1b3</citedby><cites>FETCH-LOGICAL-c4671-10bbf6ecafbe2a6b761e7cc947b09010697abee4ba99697472ae9dd871a3fd1b3</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.1550-7408.1993.tb06111.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1550-7408.1993.tb06111.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4022426$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8401471$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>LAWRENCE, FRANÇOISE</creatorcontrib><creatorcontrib>ROBERT-GERO, MALKA</creatorcontrib><title>Distribution of Macromolecular Methylations in Promastigotes of Leishmania donovani and Impact of Sinefungin</title><title>The Journal of eukaryotic microbiology</title><addtitle>J Eukaryot Microbiol</addtitle><description>Sinefungin, an antifungal and antiparasitic nucleoside antibiotic, is a very potent antileishmanial agent both in vitro and in vivo. This molecule, structurally related to S‐adenosylmethionine, is a good competitive inhibitor of methyltransferases in vitro. The aim of this report is to analyze the impact of sinefungin on methylation pattern and the subcellular localisation of methyl groups and various methylases in promastigotes of Leishmania donovani. We have shown the presence of various methylated macromolecules in different subcellular fractions, with somewhat higher concentration in membrane fraction. In vitro, sinefungin inhibits the three main protein methylases, but in cells cultured in its presence the protein carboxylmethylations are specifically inhibited.</description><subject>Adenosine - analogs & derivatives</subject><subject>Adenosine - pharmacology</subject><subject>Animals</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Antiparasitic agents</subject><subject>Biological and medical sciences</subject><subject>Carboxylmethylation</subject><subject>cell fractionation</subject><subject>hemoflagellate</subject><subject>Leishmania donovani</subject><subject>Leishmania donovani - drug effects</subject><subject>Leishmania donovani - growth & development</subject><subject>Leishmania donovani - metabolism</subject><subject>Macromolecular Substances</subject><subject>Medical sciences</subject><subject>methylated amino acids</subject><subject>Methylation</subject><subject>Pharmacology. Drug treatments</subject><subject>protein methyltransferases</subject><subject>Protein Methyltransferases - antagonists & inhibitors</subject><subject>Protein Methyltransferases - metabolism</subject><subject>Protozoa</subject><subject>Protozoan Proteins - metabolism</subject><subject>S-adenosylmethionine</subject><subject>S-Adenosylmethionine - biosynthesis</subject><subject>S-Adenosylmethionine - metabolism</subject><subject>subcellular distribution of methyl groups</subject><subject>Subcellular Fractions - metabolism</subject><issn>1066-5234</issn><issn>1550-7408</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkctu1DAUhiNEVdrCIyBFCHWX1E4cO2aBhNrSizJQCSqW1rFz0npInCFOYObtcTTRbBHe-Ej_d65_FL2jJKXhXaxTWhQkEYyUKZUyT0dNeBDS7Yvo5CC9DDHhPCmynL2KTr1fE0J5RulxdFwyQpmgJ1F7Zf04WD2Ntndx38QrMEPf9S2aqYUhXuH4vGthVn1sXfwQRPCjfepH9DNfofXPHTgLcd27_neIYnB1fNdtwIwz8c06bCb3ZN3r6KiB1uOb5T-LHj9ff7-8TaqvN3eXn6rEMC5oQonWDUcDjcYMuBacojBGMqGJJGEnKUAjMg1ShpiJDFDWdSko5E1NdX4Wne_rbob-14R-VJ31BtsWHPaTV6KQpWRc_hOknNMwURnAD3swHMf7ARu1GWwHw05RomZP1FrNh1fz4dXsiVo8UduQ_HbpMukO60PqYkLQ3y86eANtM4Az1h8wRrKMZTxgH_fYH9vi7j8GUPfXj0U590n2BYLluD0UgOGn4iIXhfrx5UY9XN0LcruqVJX_Bb1iuio</recordid><startdate>199309</startdate><enddate>199309</enddate><creator>LAWRENCE, FRANÇOISE</creator><creator>ROBERT-GERO, MALKA</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>BSCLL</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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>199309</creationdate><title>Distribution of Macromolecular Methylations in Promastigotes of Leishmania donovani and Impact of Sinefungin</title><author>LAWRENCE, FRANÇOISE ; ROBERT-GERO, MALKA</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4671-10bbf6ecafbe2a6b761e7cc947b09010697abee4ba99697472ae9dd871a3fd1b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Adenosine - analogs & derivatives</topic><topic>Adenosine - pharmacology</topic><topic>Animals</topic><topic>Antibiotics. Antiinfectious agents. Antiparasitic agents</topic><topic>Antiparasitic agents</topic><topic>Biological and medical sciences</topic><topic>Carboxylmethylation</topic><topic>cell fractionation</topic><topic>hemoflagellate</topic><topic>Leishmania donovani</topic><topic>Leishmania donovani - drug effects</topic><topic>Leishmania donovani - growth & development</topic><topic>Leishmania donovani - metabolism</topic><topic>Macromolecular Substances</topic><topic>Medical sciences</topic><topic>methylated amino acids</topic><topic>Methylation</topic><topic>Pharmacology. Drug treatments</topic><topic>protein methyltransferases</topic><topic>Protein Methyltransferases - antagonists & inhibitors</topic><topic>Protein Methyltransferases - metabolism</topic><topic>Protozoa</topic><topic>Protozoan Proteins - metabolism</topic><topic>S-adenosylmethionine</topic><topic>S-Adenosylmethionine - biosynthesis</topic><topic>S-Adenosylmethionine - metabolism</topic><topic>subcellular distribution of methyl groups</topic><topic>Subcellular Fractions - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LAWRENCE, FRANÇOISE</creatorcontrib><creatorcontrib>ROBERT-GERO, MALKA</creatorcontrib><collection>Istex</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>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of eukaryotic microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>LAWRENCE, FRANÇOISE</au><au>ROBERT-GERO, MALKA</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Distribution of Macromolecular Methylations in Promastigotes of Leishmania donovani and Impact of Sinefungin</atitle><jtitle>The Journal of eukaryotic microbiology</jtitle><addtitle>J Eukaryot Microbiol</addtitle><date>1993-09</date><risdate>1993</risdate><volume>40</volume><issue>5</issue><spage>581</spage><epage>589</epage><pages>581-589</pages><issn>1066-5234</issn><eissn>1550-7408</eissn><coden>JEMIED</coden><abstract>Sinefungin, an antifungal and antiparasitic nucleoside antibiotic, is a very potent antileishmanial agent both in vitro and in vivo. This molecule, structurally related to S‐adenosylmethionine, is a good competitive inhibitor of methyltransferases in vitro. The aim of this report is to analyze the impact of sinefungin on methylation pattern and the subcellular localisation of methyl groups and various methylases in promastigotes of Leishmania donovani. We have shown the presence of various methylated macromolecules in different subcellular fractions, with somewhat higher concentration in membrane fraction. In vitro, sinefungin inhibits the three main protein methylases, but in cells cultured in its presence the protein carboxylmethylations are specifically inhibited.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>8401471</pmid><doi>10.1111/j.1550-7408.1993.tb06111.x</doi><tpages>9</tpages></addata></record> |
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| subjects | Adenosine - analogs & derivatives Adenosine - pharmacology Animals Antibiotics. Antiinfectious agents. Antiparasitic agents Antiparasitic agents Biological and medical sciences Carboxylmethylation cell fractionation hemoflagellate Leishmania donovani Leishmania donovani - drug effects Leishmania donovani - growth & development Leishmania donovani - metabolism Macromolecular Substances Medical sciences methylated amino acids Methylation Pharmacology. Drug treatments protein methyltransferases Protein Methyltransferases - antagonists & inhibitors Protein Methyltransferases - metabolism Protozoa Protozoan Proteins - metabolism S-adenosylmethionine S-Adenosylmethionine - biosynthesis S-Adenosylmethionine - metabolism subcellular distribution of methyl groups Subcellular Fractions - metabolism |
| title | Distribution of Macromolecular Methylations in Promastigotes of Leishmania donovani and Impact of Sinefungin |
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