Molecular cloning, characterization, and heterologous expression of an acetyl-CoA acetyl transferase gene from Sanghuangporus baumii
Acetyl-CoA C-acetyltransferase synthase gene (AACT) cDNA, DNA and promoter were cloned from Sanghuangporus baumii. The gene ORF (1260 bp) encoded 419 amino acids. The AACT DNA includes five exons (1–84 bp, 140–513 bp, 570–1027 bp, 1090–1282 bp, 1344–1494 bp) and four introns (85–139 bp, 514–569 bp,...
Gespeichert in:
| Veröffentlicht in: | Protein expression and purification 2020-06, Vol.170, p.105592-105592, Article 105592 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 105592 |
|---|---|
| container_issue | |
| container_start_page | 105592 |
| container_title | Protein expression and purification |
| container_volume | 170 |
| creator | Wang, Xutong Wang, Shixin Xu, Xinru Sun, Jian Ma, Yisha Liu, Zengcai Sun, Tingting Zou, Li |
| description | Acetyl-CoA C-acetyltransferase synthase gene (AACT) cDNA, DNA and promoter were cloned from Sanghuangporus baumii. The gene ORF (1260 bp) encoded 419 amino acids. The AACT DNA includes five exons (1–84 bp, 140–513 bp, 570–1027 bp, 1090–1282 bp, 1344–1494 bp) and four introns (85–139 bp, 514–569 bp, 1028–1089 bp, 1283–1343 bp). The molecular weight of AACT protein is 43.40 kDa, it is hydrophilic with a theoretical isoelectric point of 8.96. Furthermore, The region of the transcription start site is 1997–2047 bp of AACT promoter, and it contained promoter elements (TATA Boxs, CAAT Boxs, CAAT-box, ABRE, G-Boxs, Sp1, MSA-like, LTR). AACT recombinant protein (43.40 KDa + Tag protein 22.68 KDa) was subjected in SDS-PAGE. AACT the transcription levels of in different development stages were investigated. The expression of AACT in primordia (2.4-fold) and 15 d mycelia (2.3- fold) were significantly higher than 9 d mycelia (contral). The expression level of the AACT downstream genes and triterpenoids content were determined at different developmental stages. Triterpenoid content reached its peak on day 15(7.21 mg/g). |
| doi_str_mv | 10.1016/j.pep.2020.105592 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2352642536</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1046592820300528</els_id><sourcerecordid>2352642536</sourcerecordid><originalsourceid>FETCH-LOGICAL-c353t-3fc16faa73a5d805e752479ca626559ea647a256dbaedecefc04332789f31e753</originalsourceid><addsrcrecordid>eNp9kEtv1DAUhS0Eoi9-ABvkJYtm8CN2JuqqGkFbqYgFdG3dca5nPErsYCcVZc0Px6OZdtmNfR_nHul8hHzkbMEZ1192ixHHhWBi3yvVijfklLNWV0w07dt9XeuqjJcn5CznHWOca6bekxMpmBRNw07Jv--xRzv3kKjtY_Bhc0ntFhLYCZP_C5OP4ZJC6OgWyyT2cRPnTPHPmDDnsqTRlTUFi9NTX63i9bGkU4KQHSbISDcYkLoUB_oTwmY7l2eMqfisYR68vyDvHPQZPxz_c_Lw7euv1W11_-PmbnV9X1mp5FRJZ7l2AI0E1S2ZwkaJumktaKFLegRdNyCU7taAHVp0ltWy5Fy2TvIilufk88F3TPH3jHkyg88W-x4CllRGSCV0LZTURcoPUptizgmdGZMfID0ZzswevtmZAt_s4ZsD_HLz6Wg_rwfsXi6eaRfB1UGAJeSjx2Sy9Rgsdj6hnUwX_Sv2_wFPV5eK</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2352642536</pqid></control><display><type>article</type><title>Molecular cloning, characterization, and heterologous expression of an acetyl-CoA acetyl transferase gene from Sanghuangporus baumii</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Wang, Xutong ; Wang, Shixin ; Xu, Xinru ; Sun, Jian ; Ma, Yisha ; Liu, Zengcai ; Sun, Tingting ; Zou, Li</creator><creatorcontrib>Wang, Xutong ; Wang, Shixin ; Xu, Xinru ; Sun, Jian ; Ma, Yisha ; Liu, Zengcai ; Sun, Tingting ; Zou, Li</creatorcontrib><description>Acetyl-CoA C-acetyltransferase synthase gene (AACT) cDNA, DNA and promoter were cloned from Sanghuangporus baumii. The gene ORF (1260 bp) encoded 419 amino acids. The AACT DNA includes five exons (1–84 bp, 140–513 bp, 570–1027 bp, 1090–1282 bp, 1344–1494 bp) and four introns (85–139 bp, 514–569 bp, 1028–1089 bp, 1283–1343 bp). The molecular weight of AACT protein is 43.40 kDa, it is hydrophilic with a theoretical isoelectric point of 8.96. Furthermore, The region of the transcription start site is 1997–2047 bp of AACT promoter, and it contained promoter elements (TATA Boxs, CAAT Boxs, CAAT-box, ABRE, G-Boxs, Sp1, MSA-like, LTR). AACT recombinant protein (43.40 KDa + Tag protein 22.68 KDa) was subjected in SDS-PAGE. AACT the transcription levels of in different development stages were investigated. The expression of AACT in primordia (2.4-fold) and 15 d mycelia (2.3- fold) were significantly higher than 9 d mycelia (contral). The expression level of the AACT downstream genes and triterpenoids content were determined at different developmental stages. Triterpenoid content reached its peak on day 15(7.21 mg/g).</description><identifier>ISSN: 1046-5928</identifier><identifier>EISSN: 1096-0279</identifier><identifier>DOI: 10.1016/j.pep.2020.105592</identifier><identifier>PMID: 32032770</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acetyl Coenzyme A - chemistry ; Acetyl Coenzyme A - metabolism ; Acetyl-CoA C-acetyltransferase ; Acetyl-CoA C-Acetyltransferase - chemistry ; Acetyl-CoA C-Acetyltransferase - genetics ; Acetyl-CoA C-Acetyltransferase - metabolism ; Basidiomycota - chemistry ; Basidiomycota - enzymology ; Cloning, Molecular ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Exons ; Exons and introns ; Fruiting Bodies, Fungal - chemistry ; Fruiting Bodies, Fungal - enzymology ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Gene Expression ; Genetic Vectors - chemistry ; Genetic Vectors - metabolism ; Hydrophobic and Hydrophilic Interactions ; Introns ; Isoelectric Point ; Models, Molecular ; Molecular Weight ; Mycelium - chemistry ; Mycelium - enzymology ; Open Reading Frames ; Phylogeny ; Promoter ; Promoter Regions, Genetic ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Quantitative real-time PCR ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Sanghuangporus baumii ; Triterpenes - isolation & purification ; Triterpenes - metabolism ; Triterpenoids</subject><ispartof>Protein expression and purification, 2020-06, Vol.170, p.105592-105592, Article 105592</ispartof><rights>2020 Elsevier Inc.</rights><rights>Copyright © 2020 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c353t-3fc16faa73a5d805e752479ca626559ea647a256dbaedecefc04332789f31e753</citedby><cites>FETCH-LOGICAL-c353t-3fc16faa73a5d805e752479ca626559ea647a256dbaedecefc04332789f31e753</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.pep.2020.105592$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32032770$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Xutong</creatorcontrib><creatorcontrib>Wang, Shixin</creatorcontrib><creatorcontrib>Xu, Xinru</creatorcontrib><creatorcontrib>Sun, Jian</creatorcontrib><creatorcontrib>Ma, Yisha</creatorcontrib><creatorcontrib>Liu, Zengcai</creatorcontrib><creatorcontrib>Sun, Tingting</creatorcontrib><creatorcontrib>Zou, Li</creatorcontrib><title>Molecular cloning, characterization, and heterologous expression of an acetyl-CoA acetyl transferase gene from Sanghuangporus baumii</title><title>Protein expression and purification</title><addtitle>Protein Expr Purif</addtitle><description>Acetyl-CoA C-acetyltransferase synthase gene (AACT) cDNA, DNA and promoter were cloned from Sanghuangporus baumii. The gene ORF (1260 bp) encoded 419 amino acids. The AACT DNA includes five exons (1–84 bp, 140–513 bp, 570–1027 bp, 1090–1282 bp, 1344–1494 bp) and four introns (85–139 bp, 514–569 bp, 1028–1089 bp, 1283–1343 bp). The molecular weight of AACT protein is 43.40 kDa, it is hydrophilic with a theoretical isoelectric point of 8.96. Furthermore, The region of the transcription start site is 1997–2047 bp of AACT promoter, and it contained promoter elements (TATA Boxs, CAAT Boxs, CAAT-box, ABRE, G-Boxs, Sp1, MSA-like, LTR). AACT recombinant protein (43.40 KDa + Tag protein 22.68 KDa) was subjected in SDS-PAGE. AACT the transcription levels of in different development stages were investigated. The expression of AACT in primordia (2.4-fold) and 15 d mycelia (2.3- fold) were significantly higher than 9 d mycelia (contral). The expression level of the AACT downstream genes and triterpenoids content were determined at different developmental stages. Triterpenoid content reached its peak on day 15(7.21 mg/g).</description><subject>Acetyl Coenzyme A - chemistry</subject><subject>Acetyl Coenzyme A - metabolism</subject><subject>Acetyl-CoA C-acetyltransferase</subject><subject>Acetyl-CoA C-Acetyltransferase - chemistry</subject><subject>Acetyl-CoA C-Acetyltransferase - genetics</subject><subject>Acetyl-CoA C-Acetyltransferase - metabolism</subject><subject>Basidiomycota - chemistry</subject><subject>Basidiomycota - enzymology</subject><subject>Cloning, Molecular</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Exons</subject><subject>Exons and introns</subject><subject>Fruiting Bodies, Fungal - chemistry</subject><subject>Fruiting Bodies, Fungal - enzymology</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Gene Expression</subject><subject>Genetic Vectors - chemistry</subject><subject>Genetic Vectors - metabolism</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Introns</subject><subject>Isoelectric Point</subject><subject>Models, Molecular</subject><subject>Molecular Weight</subject><subject>Mycelium - chemistry</subject><subject>Mycelium - enzymology</subject><subject>Open Reading Frames</subject><subject>Phylogeny</subject><subject>Promoter</subject><subject>Promoter Regions, Genetic</subject><subject>Protein Conformation, alpha-Helical</subject><subject>Protein Conformation, beta-Strand</subject><subject>Quantitative real-time PCR</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sanghuangporus baumii</subject><subject>Triterpenes - isolation & purification</subject><subject>Triterpenes - metabolism</subject><subject>Triterpenoids</subject><issn>1046-5928</issn><issn>1096-0279</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtv1DAUhS0Eoi9-ABvkJYtm8CN2JuqqGkFbqYgFdG3dca5nPErsYCcVZc0Px6OZdtmNfR_nHul8hHzkbMEZ1192ixHHhWBi3yvVijfklLNWV0w07dt9XeuqjJcn5CznHWOca6bekxMpmBRNw07Jv--xRzv3kKjtY_Bhc0ntFhLYCZP_C5OP4ZJC6OgWyyT2cRPnTPHPmDDnsqTRlTUFi9NTX63i9bGkU4KQHSbISDcYkLoUB_oTwmY7l2eMqfisYR68vyDvHPQZPxz_c_Lw7euv1W11_-PmbnV9X1mp5FRJZ7l2AI0E1S2ZwkaJumktaKFLegRdNyCU7taAHVp0ltWy5Fy2TvIilufk88F3TPH3jHkyg88W-x4CllRGSCV0LZTURcoPUptizgmdGZMfID0ZzswevtmZAt_s4ZsD_HLz6Wg_rwfsXi6eaRfB1UGAJeSjx2Sy9Rgsdj6hnUwX_Sv2_wFPV5eK</recordid><startdate>202006</startdate><enddate>202006</enddate><creator>Wang, Xutong</creator><creator>Wang, Shixin</creator><creator>Xu, Xinru</creator><creator>Sun, Jian</creator><creator>Ma, Yisha</creator><creator>Liu, Zengcai</creator><creator>Sun, Tingting</creator><creator>Zou, Li</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>202006</creationdate><title>Molecular cloning, characterization, and heterologous expression of an acetyl-CoA acetyl transferase gene from Sanghuangporus baumii</title><author>Wang, Xutong ; Wang, Shixin ; Xu, Xinru ; Sun, Jian ; Ma, Yisha ; Liu, Zengcai ; Sun, Tingting ; Zou, Li</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c353t-3fc16faa73a5d805e752479ca626559ea647a256dbaedecefc04332789f31e753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Acetyl Coenzyme A - chemistry</topic><topic>Acetyl Coenzyme A - metabolism</topic><topic>Acetyl-CoA C-acetyltransferase</topic><topic>Acetyl-CoA C-Acetyltransferase - chemistry</topic><topic>Acetyl-CoA C-Acetyltransferase - genetics</topic><topic>Acetyl-CoA C-Acetyltransferase - metabolism</topic><topic>Basidiomycota - chemistry</topic><topic>Basidiomycota - enzymology</topic><topic>Cloning, Molecular</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Exons</topic><topic>Exons and introns</topic><topic>Fruiting Bodies, Fungal - chemistry</topic><topic>Fruiting Bodies, Fungal - enzymology</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Gene Expression</topic><topic>Genetic Vectors - chemistry</topic><topic>Genetic Vectors - metabolism</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Introns</topic><topic>Isoelectric Point</topic><topic>Models, Molecular</topic><topic>Molecular Weight</topic><topic>Mycelium - chemistry</topic><topic>Mycelium - enzymology</topic><topic>Open Reading Frames</topic><topic>Phylogeny</topic><topic>Promoter</topic><topic>Promoter Regions, Genetic</topic><topic>Protein Conformation, alpha-Helical</topic><topic>Protein Conformation, beta-Strand</topic><topic>Quantitative real-time PCR</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sanghuangporus baumii</topic><topic>Triterpenes - isolation & purification</topic><topic>Triterpenes - metabolism</topic><topic>Triterpenoids</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Xutong</creatorcontrib><creatorcontrib>Wang, Shixin</creatorcontrib><creatorcontrib>Xu, Xinru</creatorcontrib><creatorcontrib>Sun, Jian</creatorcontrib><creatorcontrib>Ma, Yisha</creatorcontrib><creatorcontrib>Liu, Zengcai</creatorcontrib><creatorcontrib>Sun, Tingting</creatorcontrib><creatorcontrib>Zou, Li</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Protein expression and purification</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Xutong</au><au>Wang, Shixin</au><au>Xu, Xinru</au><au>Sun, Jian</au><au>Ma, Yisha</au><au>Liu, Zengcai</au><au>Sun, Tingting</au><au>Zou, Li</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning, characterization, and heterologous expression of an acetyl-CoA acetyl transferase gene from Sanghuangporus baumii</atitle><jtitle>Protein expression and purification</jtitle><addtitle>Protein Expr Purif</addtitle><date>2020-06</date><risdate>2020</risdate><volume>170</volume><spage>105592</spage><epage>105592</epage><pages>105592-105592</pages><artnum>105592</artnum><issn>1046-5928</issn><eissn>1096-0279</eissn><abstract>Acetyl-CoA C-acetyltransferase synthase gene (AACT) cDNA, DNA and promoter were cloned from Sanghuangporus baumii. The gene ORF (1260 bp) encoded 419 amino acids. The AACT DNA includes five exons (1–84 bp, 140–513 bp, 570–1027 bp, 1090–1282 bp, 1344–1494 bp) and four introns (85–139 bp, 514–569 bp, 1028–1089 bp, 1283–1343 bp). The molecular weight of AACT protein is 43.40 kDa, it is hydrophilic with a theoretical isoelectric point of 8.96. Furthermore, The region of the transcription start site is 1997–2047 bp of AACT promoter, and it contained promoter elements (TATA Boxs, CAAT Boxs, CAAT-box, ABRE, G-Boxs, Sp1, MSA-like, LTR). AACT recombinant protein (43.40 KDa + Tag protein 22.68 KDa) was subjected in SDS-PAGE. AACT the transcription levels of in different development stages were investigated. The expression of AACT in primordia (2.4-fold) and 15 d mycelia (2.3- fold) were significantly higher than 9 d mycelia (contral). The expression level of the AACT downstream genes and triterpenoids content were determined at different developmental stages. Triterpenoid content reached its peak on day 15(7.21 mg/g).</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>32032770</pmid><doi>10.1016/j.pep.2020.105592</doi><tpages>1</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1046-5928 |
| ispartof | Protein expression and purification, 2020-06, Vol.170, p.105592-105592, Article 105592 |
| issn | 1046-5928 1096-0279 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2352642536 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Acetyl Coenzyme A - chemistry Acetyl Coenzyme A - metabolism Acetyl-CoA C-acetyltransferase Acetyl-CoA C-Acetyltransferase - chemistry Acetyl-CoA C-Acetyltransferase - genetics Acetyl-CoA C-Acetyltransferase - metabolism Basidiomycota - chemistry Basidiomycota - enzymology Cloning, Molecular Escherichia coli - genetics Escherichia coli - metabolism Exons Exons and introns Fruiting Bodies, Fungal - chemistry Fruiting Bodies, Fungal - enzymology Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Gene Expression Genetic Vectors - chemistry Genetic Vectors - metabolism Hydrophobic and Hydrophilic Interactions Introns Isoelectric Point Models, Molecular Molecular Weight Mycelium - chemistry Mycelium - enzymology Open Reading Frames Phylogeny Promoter Promoter Regions, Genetic Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Quantitative real-time PCR Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sanghuangporus baumii Triterpenes - isolation & purification Triterpenes - metabolism Triterpenoids |
| title | Molecular cloning, characterization, and heterologous expression of an acetyl-CoA acetyl transferase gene from Sanghuangporus baumii |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T17%3A22%3A32IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Molecular%20cloning,%20characterization,%20and%20heterologous%20expression%20of%20an%20acetyl-CoA%20acetyl%20transferase%20gene%20from%20Sanghuangporus%20baumii&rft.jtitle=Protein%20expression%20and%20purification&rft.au=Wang,%20Xutong&rft.date=2020-06&rft.volume=170&rft.spage=105592&rft.epage=105592&rft.pages=105592-105592&rft.artnum=105592&rft.issn=1046-5928&rft.eissn=1096-0279&rft_id=info:doi/10.1016/j.pep.2020.105592&rft_dat=%3Cproquest_cross%3E2352642536%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2352642536&rft_id=info:pmid/32032770&rft_els_id=S1046592820300528&rfr_iscdi=true |