Characterization of a farnesyl diphosphate synthase gene from Penicillium brevicompactum MUCL 19011
OBJECTIVES: Farnesyl diphosphate synthase is a critical enzyme in the isoprenoids biosynthesis pathway responsible for ergosterol and secondary metabolites biosynthesis in fungi. RESULTS: Characterization of fds from Penicillium brevicompactum (Pbfds) was performed using TAIL-PCR and RT-PCR followed...
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Veröffentlicht in: | Biotechnology letters 2016-01, Vol.38 (1), p.71-79 |
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creator | Sharifirad, Atefeh Mohammadian, Somayeh Yakhchali, Bagher Mehrpooyan, Sina Fatemi, Seyed Safa-ali |
description | OBJECTIVES: Farnesyl diphosphate synthase is a critical enzyme in the isoprenoids biosynthesis pathway responsible for ergosterol and secondary metabolites biosynthesis in fungi. RESULTS: Characterization of fds from Penicillium brevicompactum (Pbfds) was performed using TAIL-PCR and RT-PCR followed by complementation tests in Saccharomyces cerevisiae and determination of its expression profile by semi-quantitative RT-PCR. Promoter analysis suggests some binding sites for transcription factors some of which are involved in fungal growth and response to environmental stress. The Pbfds ORF encodes a cytosolic 39.7 kDa protein with a high conservation among Eurotiomycetes and the highest identity (96 %) with Pen. chrysogenum. Homology-based structural modeling suggests that the PbFDS is formed by the arrangement of 15 core helices around a large central cavity where the catalytic reaction takes place. Superimposition of the predicted 3D structure of the enzyme on its ortholog in human reveals the same folding pattern in the counterparts. CONCLUSION: The Pbfds expression may be stimulated in response to the environmental stresses and fungal growth and encodes the PBFDS—a cytosolic enzyme which with a key role in ergosterol and secondary metabolites biosynthesis. |
doi_str_mv | 10.1007/s10529-015-1943-9 |
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RESULTS: Characterization of fds from Penicillium brevicompactum (Pbfds) was performed using TAIL-PCR and RT-PCR followed by complementation tests in Saccharomyces cerevisiae and determination of its expression profile by semi-quantitative RT-PCR. Promoter analysis suggests some binding sites for transcription factors some of which are involved in fungal growth and response to environmental stress. The Pbfds ORF encodes a cytosolic 39.7 kDa protein with a high conservation among Eurotiomycetes and the highest identity (96 %) with Pen. chrysogenum. Homology-based structural modeling suggests that the PbFDS is formed by the arrangement of 15 core helices around a large central cavity where the catalytic reaction takes place. Superimposition of the predicted 3D structure of the enzyme on its ortholog in human reveals the same folding pattern in the counterparts. CONCLUSION: The Pbfds expression may be stimulated in response to the environmental stresses and fungal growth and encodes the PBFDS—a cytosolic enzyme which with a key role in ergosterol and secondary metabolites biosynthesis.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-015-1943-9</identifier><identifier>PMID: 26334936</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Applied Microbiology ; Binding Sites ; Biochemistry ; Biomedical and Life Sciences ; Biosynthesis ; Biotechnology ; Chemical synthesis ; Cloning, Molecular - methods ; Diphosphates ; Environmental stress ; Enzymes ; ergosterol ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Fungi ; Gene Expression Profiling - methods ; genes ; Geranyltranstransferase - chemistry ; Geranyltranstransferase - genetics ; Geranyltranstransferase - metabolism ; humans ; isoprenoids ; Life Sciences ; Mathematical models ; Metabolites ; microbial growth ; Microbiology ; Models, Molecular ; open reading frames ; Original Research Paper ; Penicillium ; Penicillium - enzymology ; Penicillium - genetics ; Penicillium brevicompactum ; Phosphates ; Promoter Regions, Genetic ; reverse transcriptase polymerase chain reaction ; Saccharomyces cerevisiae ; Secondary metabolites ; Stresses ; transcription factors ; Transcription Factors - metabolism</subject><ispartof>Biotechnology letters, 2016-01, Vol.38 (1), p.71-79</ispartof><rights>Springer Science+Business Media Dordrecht 2015</rights><rights>Springer Science+Business Media Dordrecht 2016</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c532t-4dac5c9dcc262ab65c22a54b161fca86aea03a73a962240e86815163609ab8c33</citedby><cites>FETCH-LOGICAL-c532t-4dac5c9dcc262ab65c22a54b161fca86aea03a73a962240e86815163609ab8c33</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/s10529-015-1943-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10529-015-1943-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26334936$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sharifirad, Atefeh</creatorcontrib><creatorcontrib>Mohammadian, Somayeh</creatorcontrib><creatorcontrib>Yakhchali, Bagher</creatorcontrib><creatorcontrib>Mehrpooyan, Sina</creatorcontrib><creatorcontrib>Fatemi, Seyed Safa-ali</creatorcontrib><title>Characterization of a farnesyl diphosphate synthase gene from Penicillium brevicompactum MUCL 19011</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><addtitle>Biotechnol Lett</addtitle><description>OBJECTIVES: Farnesyl diphosphate synthase is a critical enzyme in the isoprenoids biosynthesis pathway responsible for ergosterol and secondary metabolites biosynthesis in fungi. RESULTS: Characterization of fds from Penicillium brevicompactum (Pbfds) was performed using TAIL-PCR and RT-PCR followed by complementation tests in Saccharomyces cerevisiae and determination of its expression profile by semi-quantitative RT-PCR. Promoter analysis suggests some binding sites for transcription factors some of which are involved in fungal growth and response to environmental stress. The Pbfds ORF encodes a cytosolic 39.7 kDa protein with a high conservation among Eurotiomycetes and the highest identity (96 %) with Pen. chrysogenum. Homology-based structural modeling suggests that the PbFDS is formed by the arrangement of 15 core helices around a large central cavity where the catalytic reaction takes place. Superimposition of the predicted 3D structure of the enzyme on its ortholog in human reveals the same folding pattern in the counterparts. CONCLUSION: The Pbfds expression may be stimulated in response to the environmental stresses and fungal growth and encodes the PBFDS—a cytosolic enzyme which with a key role in ergosterol and secondary metabolites biosynthesis.</description><subject>Applied Microbiology</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biosynthesis</subject><subject>Biotechnology</subject><subject>Chemical synthesis</subject><subject>Cloning, Molecular - methods</subject><subject>Diphosphates</subject><subject>Environmental stress</subject><subject>Enzymes</subject><subject>ergosterol</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Fungi</subject><subject>Gene Expression Profiling - methods</subject><subject>genes</subject><subject>Geranyltranstransferase - chemistry</subject><subject>Geranyltranstransferase - genetics</subject><subject>Geranyltranstransferase - metabolism</subject><subject>humans</subject><subject>isoprenoids</subject><subject>Life Sciences</subject><subject>Mathematical models</subject><subject>Metabolites</subject><subject>microbial growth</subject><subject>Microbiology</subject><subject>Models, Molecular</subject><subject>open reading frames</subject><subject>Original Research Paper</subject><subject>Penicillium</subject><subject>Penicillium - enzymology</subject><subject>Penicillium - genetics</subject><subject>Penicillium brevicompactum</subject><subject>Phosphates</subject><subject>Promoter Regions, Genetic</subject><subject>reverse transcriptase polymerase chain reaction</subject><subject>Saccharomyces cerevisiae</subject><subject>Secondary metabolites</subject><subject>Stresses</subject><subject>transcription factors</subject><subject>Transcription Factors - metabolism</subject><issn>0141-5492</issn><issn>1573-6776</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><recordid>eNqNkkur1DAYhoMonnH0B7jRghs31Xy5NksZvMGIgs46fM2kMzm0TU1aYfz15tCjiAs5qxDyvG8uTwh5CvQVUKpfZ6CSmZqCrMEIXpt7ZANS81ppre6TDQUBtRSGXZFHOV9TSo2m-iG5YopzYbjaELc7Y0I3-xR-4hziWMWuwqrDNPp86atjmM4xT2ecfZUv43zG7KuTH33VpThUX_wYXOj7sAxVm_yP4OIwlboy_XTY7SswFOAxedBhn_2T23FLDu_eftt9qPef33_cvdnXTnI21-KITjpzdI4phq2SjjGUogUFncNGoUfKUXM0ijFBfaMakKC4ogbbxnG-JS_X3inF74vPsx1Cdr7vcfRxyRa04YwxLdgdUCWNVkLDXVDaGGjKm27Ji3_Q67iksdy5UFIyUc4qCgUr5VLMOfnOTikMmC4WqL3xalevtni1N16tKZlnt81LO_jjn8RvkQVgK5DL0njy6a-t_9P6fA11GC2eUsj28JVRUOWnCEaV4L8AZ2O0lA</recordid><startdate>20160101</startdate><enddate>20160101</enddate><creator>Sharifirad, Atefeh</creator><creator>Mohammadian, Somayeh</creator><creator>Yakhchali, Bagher</creator><creator>Mehrpooyan, Sina</creator><creator>Fatemi, Seyed Safa-ali</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>FBQ</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>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</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>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</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><scope>7QO</scope></search><sort><creationdate>20160101</creationdate><title>Characterization of a farnesyl diphosphate synthase gene from Penicillium brevicompactum MUCL 19011</title><author>Sharifirad, Atefeh ; Mohammadian, Somayeh ; Yakhchali, Bagher ; Mehrpooyan, Sina ; Fatemi, Seyed Safa-ali</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c532t-4dac5c9dcc262ab65c22a54b161fca86aea03a73a962240e86815163609ab8c33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Applied Microbiology</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biosynthesis</topic><topic>Biotechnology</topic><topic>Chemical synthesis</topic><topic>Cloning, Molecular - methods</topic><topic>Diphosphates</topic><topic>Environmental stress</topic><topic>Enzymes</topic><topic>ergosterol</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Fungi</topic><topic>Gene Expression Profiling - methods</topic><topic>genes</topic><topic>Geranyltranstransferase - chemistry</topic><topic>Geranyltranstransferase - genetics</topic><topic>Geranyltranstransferase - metabolism</topic><topic>humans</topic><topic>isoprenoids</topic><topic>Life Sciences</topic><topic>Mathematical models</topic><topic>Metabolites</topic><topic>microbial growth</topic><topic>Microbiology</topic><topic>Models, Molecular</topic><topic>open reading frames</topic><topic>Original Research Paper</topic><topic>Penicillium</topic><topic>Penicillium - enzymology</topic><topic>Penicillium - genetics</topic><topic>Penicillium brevicompactum</topic><topic>Phosphates</topic><topic>Promoter Regions, Genetic</topic><topic>reverse transcriptase polymerase chain reaction</topic><topic>Saccharomyces cerevisiae</topic><topic>Secondary metabolites</topic><topic>Stresses</topic><topic>transcription factors</topic><topic>Transcription Factors - 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Academic</collection><collection>Biotechnology Research Abstracts</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sharifirad, Atefeh</au><au>Mohammadian, Somayeh</au><au>Yakhchali, Bagher</au><au>Mehrpooyan, Sina</au><au>Fatemi, Seyed Safa-ali</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a farnesyl diphosphate synthase gene from Penicillium brevicompactum MUCL 19011</atitle><jtitle>Biotechnology letters</jtitle><stitle>Biotechnol Lett</stitle><addtitle>Biotechnol Lett</addtitle><date>2016-01-01</date><risdate>2016</risdate><volume>38</volume><issue>1</issue><spage>71</spage><epage>79</epage><pages>71-79</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><abstract>OBJECTIVES: Farnesyl diphosphate synthase is a critical enzyme in the isoprenoids biosynthesis pathway responsible for ergosterol and secondary metabolites biosynthesis in fungi. RESULTS: Characterization of fds from Penicillium brevicompactum (Pbfds) was performed using TAIL-PCR and RT-PCR followed by complementation tests in Saccharomyces cerevisiae and determination of its expression profile by semi-quantitative RT-PCR. Promoter analysis suggests some binding sites for transcription factors some of which are involved in fungal growth and response to environmental stress. The Pbfds ORF encodes a cytosolic 39.7 kDa protein with a high conservation among Eurotiomycetes and the highest identity (96 %) with Pen. chrysogenum. Homology-based structural modeling suggests that the PbFDS is formed by the arrangement of 15 core helices around a large central cavity where the catalytic reaction takes place. Superimposition of the predicted 3D structure of the enzyme on its ortholog in human reveals the same folding pattern in the counterparts. CONCLUSION: The Pbfds expression may be stimulated in response to the environmental stresses and fungal growth and encodes the PBFDS—a cytosolic enzyme which with a key role in ergosterol and secondary metabolites biosynthesis.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>26334936</pmid><doi>10.1007/s10529-015-1943-9</doi><tpages>9</tpages></addata></record> |
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subjects | Applied Microbiology Binding Sites Biochemistry Biomedical and Life Sciences Biosynthesis Biotechnology Chemical synthesis Cloning, Molecular - methods Diphosphates Environmental stress Enzymes ergosterol Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Fungi Gene Expression Profiling - methods genes Geranyltranstransferase - chemistry Geranyltranstransferase - genetics Geranyltranstransferase - metabolism humans isoprenoids Life Sciences Mathematical models Metabolites microbial growth Microbiology Models, Molecular open reading frames Original Research Paper Penicillium Penicillium - enzymology Penicillium - genetics Penicillium brevicompactum Phosphates Promoter Regions, Genetic reverse transcriptase polymerase chain reaction Saccharomyces cerevisiae Secondary metabolites Stresses transcription factors Transcription Factors - metabolism |
title | Characterization of a farnesyl diphosphate synthase gene from Penicillium brevicompactum MUCL 19011 |
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