Molecular Cloning and Characterization of O-Methyltransferase from Mango Fruit (Mangifera indica cv. Alphonso)
Flavour of ripe Alphonso mango is invariably dominated by the de novo appearance of lactones and furanones during ripening. Of these, furanones comprising furaneol (4-hydroxy-2,5-dimethyl-3(2H)-furanone) and mesifuran (2,5-dimethyl-4-methoxy-3(2H)-furanone) are of particular importance due to their...
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creator | Chidley, Hemangi G. Oak, Pranjali S. Deshpande, Ashish B. Pujari, Keshav H. Giri, Ashok P. Gupta, Vidya S. |
description | Flavour of ripe Alphonso mango is invariably dominated by the de novo appearance of lactones and furanones during ripening. Of these, furanones comprising furaneol (4-hydroxy-2,5-dimethyl-3(2H)-furanone) and mesifuran (2,5-dimethyl-4-methoxy-3(2H)-furanone) are of particular importance due to their sweet, fruity caramel-like flavour characters and low odour detection thresholds. We isolated a 1056 bp complete open reading frame of a cDNA encoding
S
-adenosyl-
l
-methionine-dependent
O
-methyltransferase from Alphonso mango. The recombinantly expressed enzyme,
MiO
MTS showed substrate specificity towards furaneol and protocatechuic aldehyde synthesizing mesifuran and vanillin, respectively, in an in vitro assay reaction. A semi-quantitative PCR analysis showed fruit-specific expression of
MiOMTS
transcripts. Quantitative real-time PCR displayed ripening-related expression pattern of
MiOMTS
in both pulp and skin of Alphonso mango. Also, early and significantly enhanced accumulation of its transcripts was detected in pulp and skin of ethylene-treated fruits. Ripening-related and fruit-specific expression profile of
MiOMTS
and substrate specificity towards furaneol is a suggestive of its involvement in the synthesis of mesifuran in Alphonso mango. Moreover, a significant trigger in the expression of
MiOMTS
transcripts in ethylene-treated fruits point towards the transcriptional regulation of mesifuran biosynthesis by ethylene. |
doi_str_mv | 10.1007/s12033-016-9933-2 |
format | Article |
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S
-adenosyl-
l
-methionine-dependent
O
-methyltransferase from Alphonso mango. The recombinantly expressed enzyme,
MiO
MTS showed substrate specificity towards furaneol and protocatechuic aldehyde synthesizing mesifuran and vanillin, respectively, in an in vitro assay reaction. A semi-quantitative PCR analysis showed fruit-specific expression of
MiOMTS
transcripts. Quantitative real-time PCR displayed ripening-related expression pattern of
MiOMTS
in both pulp and skin of Alphonso mango. Also, early and significantly enhanced accumulation of its transcripts was detected in pulp and skin of ethylene-treated fruits. Ripening-related and fruit-specific expression profile of
MiOMTS
and substrate specificity towards furaneol is a suggestive of its involvement in the synthesis of mesifuran in Alphonso mango. Moreover, a significant trigger in the expression of
MiOMTS
transcripts in ethylene-treated fruits point towards the transcriptional regulation of mesifuran biosynthesis by ethylene.</description><identifier>ISSN: 1073-6085</identifier><identifier>EISSN: 1559-0305</identifier><identifier>DOI: 10.1007/s12033-016-9933-2</identifier><identifier>PMID: 27039187</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Amino Acid Sequence ; Biochemistry ; Biological Techniques ; Biosynthesis ; Biotechnology ; Cell Biology ; Chemistry ; Chemistry and Materials Science ; Cloning ; Cloning, Molecular ; DNA, Complementary - genetics ; Enzymes ; Fruits ; Human Genetics ; Mangifera - enzymology ; Mangifera indica ; Methyltransferases - chemistry ; Methyltransferases - genetics ; Methyltransferases - metabolism ; Original Paper ; Protein Science ; Sequence Homology, Amino Acid</subject><ispartof>Molecular biotechnology, 2016-05, Vol.58 (5), p.340-350</ispartof><rights>Springer Science+Business Media New York 2016</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c471t-7c6fb15f002114de3617f1e8dc35b9ab7961c8dd39ac05e9f259ab1784e92b23</citedby><cites>FETCH-LOGICAL-c471t-7c6fb15f002114de3617f1e8dc35b9ab7961c8dd39ac05e9f259ab1784e92b23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12033-016-9933-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12033-016-9933-2$$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/27039187$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chidley, Hemangi G.</creatorcontrib><creatorcontrib>Oak, Pranjali S.</creatorcontrib><creatorcontrib>Deshpande, Ashish B.</creatorcontrib><creatorcontrib>Pujari, Keshav H.</creatorcontrib><creatorcontrib>Giri, Ashok P.</creatorcontrib><creatorcontrib>Gupta, Vidya S.</creatorcontrib><title>Molecular Cloning and Characterization of O-Methyltransferase from Mango Fruit (Mangifera indica cv. Alphonso)</title><title>Molecular biotechnology</title><addtitle>Mol Biotechnol</addtitle><addtitle>Mol Biotechnol</addtitle><description>Flavour of ripe Alphonso mango is invariably dominated by the de novo appearance of lactones and furanones during ripening. Of these, furanones comprising furaneol (4-hydroxy-2,5-dimethyl-3(2H)-furanone) and mesifuran (2,5-dimethyl-4-methoxy-3(2H)-furanone) are of particular importance due to their sweet, fruity caramel-like flavour characters and low odour detection thresholds. We isolated a 1056 bp complete open reading frame of a cDNA encoding
S
-adenosyl-
l
-methionine-dependent
O
-methyltransferase from Alphonso mango. The recombinantly expressed enzyme,
MiO
MTS showed substrate specificity towards furaneol and protocatechuic aldehyde synthesizing mesifuran and vanillin, respectively, in an in vitro assay reaction. A semi-quantitative PCR analysis showed fruit-specific expression of
MiOMTS
transcripts. Quantitative real-time PCR displayed ripening-related expression pattern of
MiOMTS
in both pulp and skin of Alphonso mango. Also, early and significantly enhanced accumulation of its transcripts was detected in pulp and skin of ethylene-treated fruits. Ripening-related and fruit-specific expression profile of
MiOMTS
and substrate specificity towards furaneol is a suggestive of its involvement in the synthesis of mesifuran in Alphonso mango. Moreover, a significant trigger in the expression of
MiOMTS
transcripts in ethylene-treated fruits point towards the transcriptional regulation of mesifuran biosynthesis by ethylene.</description><subject>Amino Acid Sequence</subject><subject>Biochemistry</subject><subject>Biological Techniques</subject><subject>Biosynthesis</subject><subject>Biotechnology</subject><subject>Cell Biology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary - genetics</subject><subject>Enzymes</subject><subject>Fruits</subject><subject>Human Genetics</subject><subject>Mangifera - enzymology</subject><subject>Mangifera indica</subject><subject>Methyltransferases - chemistry</subject><subject>Methyltransferases - genetics</subject><subject>Methyltransferases - metabolism</subject><subject>Original Paper</subject><subject>Protein Science</subject><subject>Sequence Homology, Amino Acid</subject><issn>1073-6085</issn><issn>1559-0305</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNkUFPHCEUx0mjqVb9AF4aEi_2MMqDYRiOZlPbJm72snfCMLCLmYUVZkz008tkbWOaNOmJB-_Hn0d-CF0CuQFCxG0GShirCDSVlKWgn9ApcC4rwgg_KjURrGpIy0_Ql5wfCaHAa_YZnVBBmIRWnKKwjIM106ATXgwx-LDBOvR4sdVJm9Em_6pHHwOODq-qpR23L8OYdMjOJp0tdinu8FKHTcT3afIjvp43fu5iH3pvNDbPN_hu2G9jyPHbOTp2esj24n09Q-v77-vFz-ph9ePX4u6hMrWAsRKmcR1wN08MdW9ZA8KBbXvDeCd1J2QDpu17JrUh3EpHeTkF0dZW0o6yM3R9iN2n-DTZPKqdz8YOgw42TlkVklMOwP4LBeC0YU1Br_5CH-OUQvnHTJGaU0pFoeBAmRRzTtapffI7nV4UEDVrUwdtqmhTszY1D_H1PXnqdrb_c-O3pwLQA5BLK2xs-vD0P1PfAJ5xoXg</recordid><startdate>20160501</startdate><enddate>20160501</enddate><creator>Chidley, Hemangi G.</creator><creator>Oak, Pranjali S.</creator><creator>Deshpande, Ashish B.</creator><creator>Pujari, Keshav H.</creator><creator>Giri, Ashok P.</creator><creator>Gupta, Vidya S.</creator><general>Springer US</general><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</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>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</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>L6V</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20160501</creationdate><title>Molecular Cloning and Characterization of O-Methyltransferase from Mango Fruit (Mangifera indica cv. Alphonso)</title><author>Chidley, Hemangi G. ; Oak, Pranjali S. ; Deshpande, Ashish B. ; Pujari, Keshav H. ; Giri, Ashok P. ; Gupta, Vidya S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c471t-7c6fb15f002114de3617f1e8dc35b9ab7961c8dd39ac05e9f259ab1784e92b23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Amino Acid Sequence</topic><topic>Biochemistry</topic><topic>Biological Techniques</topic><topic>Biosynthesis</topic><topic>Biotechnology</topic><topic>Cell Biology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Cloning</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary - genetics</topic><topic>Enzymes</topic><topic>Fruits</topic><topic>Human Genetics</topic><topic>Mangifera - enzymology</topic><topic>Mangifera indica</topic><topic>Methyltransferases - chemistry</topic><topic>Methyltransferases - genetics</topic><topic>Methyltransferases - metabolism</topic><topic>Original Paper</topic><topic>Protein Science</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chidley, Hemangi G.</creatorcontrib><creatorcontrib>Oak, Pranjali S.</creatorcontrib><creatorcontrib>Deshpande, Ashish B.</creatorcontrib><creatorcontrib>Pujari, Keshav H.</creatorcontrib><creatorcontrib>Giri, Ashok P.</creatorcontrib><creatorcontrib>Gupta, Vidya S.</creatorcontrib><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>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</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>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering 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>Engineering Collection</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chidley, Hemangi G.</au><au>Oak, Pranjali S.</au><au>Deshpande, Ashish B.</au><au>Pujari, Keshav H.</au><au>Giri, Ashok P.</au><au>Gupta, Vidya S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Cloning and Characterization of O-Methyltransferase from Mango Fruit (Mangifera indica cv. Alphonso)</atitle><jtitle>Molecular biotechnology</jtitle><stitle>Mol Biotechnol</stitle><addtitle>Mol Biotechnol</addtitle><date>2016-05-01</date><risdate>2016</risdate><volume>58</volume><issue>5</issue><spage>340</spage><epage>350</epage><pages>340-350</pages><issn>1073-6085</issn><eissn>1559-0305</eissn><abstract>Flavour of ripe Alphonso mango is invariably dominated by the de novo appearance of lactones and furanones during ripening. Of these, furanones comprising furaneol (4-hydroxy-2,5-dimethyl-3(2H)-furanone) and mesifuran (2,5-dimethyl-4-methoxy-3(2H)-furanone) are of particular importance due to their sweet, fruity caramel-like flavour characters and low odour detection thresholds. We isolated a 1056 bp complete open reading frame of a cDNA encoding
S
-adenosyl-
l
-methionine-dependent
O
-methyltransferase from Alphonso mango. The recombinantly expressed enzyme,
MiO
MTS showed substrate specificity towards furaneol and protocatechuic aldehyde synthesizing mesifuran and vanillin, respectively, in an in vitro assay reaction. A semi-quantitative PCR analysis showed fruit-specific expression of
MiOMTS
transcripts. Quantitative real-time PCR displayed ripening-related expression pattern of
MiOMTS
in both pulp and skin of Alphonso mango. Also, early and significantly enhanced accumulation of its transcripts was detected in pulp and skin of ethylene-treated fruits. Ripening-related and fruit-specific expression profile of
MiOMTS
and substrate specificity towards furaneol is a suggestive of its involvement in the synthesis of mesifuran in Alphonso mango. Moreover, a significant trigger in the expression of
MiOMTS
transcripts in ethylene-treated fruits point towards the transcriptional regulation of mesifuran biosynthesis by ethylene.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>27039187</pmid><doi>10.1007/s12033-016-9933-2</doi><tpages>11</tpages></addata></record> |
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subjects | Amino Acid Sequence Biochemistry Biological Techniques Biosynthesis Biotechnology Cell Biology Chemistry Chemistry and Materials Science Cloning Cloning, Molecular DNA, Complementary - genetics Enzymes Fruits Human Genetics Mangifera - enzymology Mangifera indica Methyltransferases - chemistry Methyltransferases - genetics Methyltransferases - metabolism Original Paper Protein Science Sequence Homology, Amino Acid |
title | Molecular Cloning and Characterization of O-Methyltransferase from Mango Fruit (Mangifera indica cv. Alphonso) |
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