Altered secretion patterns and cell wall organization caused by loss of PodB function in the filamentous fungus Aspergillus nidulans
Filamentous fungi are widely used in the production of a variety of industrially relevant enzymes and proteins as they have the unique ability to secrete tremendous amounts of proteins. However, the secretory pathways in filamentous fungi are not completely understood. Here, we investigated the role...
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| Veröffentlicht in: | Scientific reports 2018-07, Vol.8 (1), p.11433-11, Article 11433 |
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| creator | Boppidi, Karthik R. Ribeiro, Liliane Fraga Costa Iambamrung, Sirasa Nelson, Sidney M. Wang, Yan Momany, Michelle Richardson, Elizabeth A. Lincoln, Stephen Srivastava, Ranjan Harris, Steven D. Marten, Mark R. |
| description | Filamentous fungi are widely used in the production of a variety of industrially relevant enzymes and proteins as they have the unique ability to secrete tremendous amounts of proteins. However, the secretory pathways in filamentous fungi are not completely understood. Here, we investigated the role of a mutation in the POlarity Defective (
podB
) gene on growth, protein secretion, and cell wall organization in
Aspergillus nidulans
using a temperature sensitive (Ts) mutant. At restrictive temperature, the mutation resulted in lack of biomass accumulation, but led to a significant increase in specific protein productivity. Proteomic analysis of the secretome showed that the relative abundance of 584 (out of 747 identified) proteins was altered due to the mutation. Of these, 517 were secreted at higher levels. Other phenotypic differences observed in the mutant include up-regulation of unfolded protein response (UPR), deformation of Golgi apparatus and uneven cell wall thickness. Furthermore, proteomic analysis of cell wall components in the mutant revealed the presence of intracellular proteins in higher abundance accompanied by lower levels of most cell wall proteins. Taken together, results from this study suggest the importance of PodB as a target when engineering fungal strains for enhanced secretion of valuable biomolecules. |
| doi_str_mv | 10.1038/s41598-018-29615-z |
| format | Article |
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podB
) gene on growth, protein secretion, and cell wall organization in
Aspergillus nidulans
using a temperature sensitive (Ts) mutant. At restrictive temperature, the mutation resulted in lack of biomass accumulation, but led to a significant increase in specific protein productivity. Proteomic analysis of the secretome showed that the relative abundance of 584 (out of 747 identified) proteins was altered due to the mutation. Of these, 517 were secreted at higher levels. Other phenotypic differences observed in the mutant include up-regulation of unfolded protein response (UPR), deformation of Golgi apparatus and uneven cell wall thickness. Furthermore, proteomic analysis of cell wall components in the mutant revealed the presence of intracellular proteins in higher abundance accompanied by lower levels of most cell wall proteins. Taken together, results from this study suggest the importance of PodB as a target when engineering fungal strains for enhanced secretion of valuable biomolecules.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-018-29615-z</identifier><identifier>PMID: 30061727</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>14/28 ; 14/34 ; 14/63 ; 38/23 ; 38/39 ; 631/326/193/2096 ; 631/61/252 ; 82/58 ; Aspergillus nidulans ; Aspergillus nidulans - cytology ; Aspergillus nidulans - genetics ; Aspergillus nidulans - growth & development ; Aspergillus nidulans - metabolism ; Cell Wall - metabolism ; Cell Wall - ultrastructure ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Fungi ; Gene Expression Regulation, Fungal ; Genotype ; Golgi cells ; Humanities and Social Sciences ; Hyphae - ultrastructure ; multidisciplinary ; Mutation ; Mutation - genetics ; Phenotype ; Polarity ; Protein folding ; Proteins ; Proteomics ; Relative abundance ; Science ; Science (multidisciplinary) ; Secretion ; Secretome ; Temperature ; Unfolded Protein Response ; Up-Regulation</subject><ispartof>Scientific reports, 2018-07, Vol.8 (1), p.11433-11, Article 11433</ispartof><rights>The Author(s) 2018</rights><rights>2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c511t-c01c90c46362dcc5b66edad889596933e02eca20db37453e5d224f75263cc98c3</citedby><cites>FETCH-LOGICAL-c511t-c01c90c46362dcc5b66edad889596933e02eca20db37453e5d224f75263cc98c3</cites><orcidid>0000-0003-4309-605X</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/PMC6065416/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6065416/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,41120,42189,51576,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30061727$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Boppidi, Karthik R.</creatorcontrib><creatorcontrib>Ribeiro, Liliane Fraga Costa</creatorcontrib><creatorcontrib>Iambamrung, Sirasa</creatorcontrib><creatorcontrib>Nelson, Sidney M.</creatorcontrib><creatorcontrib>Wang, Yan</creatorcontrib><creatorcontrib>Momany, Michelle</creatorcontrib><creatorcontrib>Richardson, Elizabeth A.</creatorcontrib><creatorcontrib>Lincoln, Stephen</creatorcontrib><creatorcontrib>Srivastava, Ranjan</creatorcontrib><creatorcontrib>Harris, Steven D.</creatorcontrib><creatorcontrib>Marten, Mark R.</creatorcontrib><title>Altered secretion patterns and cell wall organization caused by loss of PodB function in the filamentous fungus Aspergillus nidulans</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Filamentous fungi are widely used in the production of a variety of industrially relevant enzymes and proteins as they have the unique ability to secrete tremendous amounts of proteins. However, the secretory pathways in filamentous fungi are not completely understood. Here, we investigated the role of a mutation in the POlarity Defective (
podB
) gene on growth, protein secretion, and cell wall organization in
Aspergillus nidulans
using a temperature sensitive (Ts) mutant. At restrictive temperature, the mutation resulted in lack of biomass accumulation, but led to a significant increase in specific protein productivity. Proteomic analysis of the secretome showed that the relative abundance of 584 (out of 747 identified) proteins was altered due to the mutation. Of these, 517 were secreted at higher levels. Other phenotypic differences observed in the mutant include up-regulation of unfolded protein response (UPR), deformation of Golgi apparatus and uneven cell wall thickness. Furthermore, proteomic analysis of cell wall components in the mutant revealed the presence of intracellular proteins in higher abundance accompanied by lower levels of most cell wall proteins. Taken together, results from this study suggest the importance of PodB as a target when engineering fungal strains for enhanced secretion of valuable biomolecules.</description><subject>14/28</subject><subject>14/34</subject><subject>14/63</subject><subject>38/23</subject><subject>38/39</subject><subject>631/326/193/2096</subject><subject>631/61/252</subject><subject>82/58</subject><subject>Aspergillus nidulans</subject><subject>Aspergillus nidulans - cytology</subject><subject>Aspergillus nidulans - genetics</subject><subject>Aspergillus nidulans - growth & development</subject><subject>Aspergillus nidulans - metabolism</subject><subject>Cell Wall - metabolism</subject><subject>Cell Wall - ultrastructure</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Fungi</subject><subject>Gene Expression Regulation, Fungal</subject><subject>Genotype</subject><subject>Golgi cells</subject><subject>Humanities and Social Sciences</subject><subject>Hyphae - ultrastructure</subject><subject>multidisciplinary</subject><subject>Mutation</subject><subject>Mutation - genetics</subject><subject>Phenotype</subject><subject>Polarity</subject><subject>Protein folding</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Relative abundance</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Secretion</subject><subject>Secretome</subject><subject>Temperature</subject><subject>Unfolded Protein Response</subject><subject>Up-Regulation</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><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>eNp9UT1vFDEQtRCIRCF_gAJZoqFZ8PeuG6Qj4kuKBAXUls-e3Tjy2Ye9C8rV_HB8dyEEClx4Rn5vnmfmIfSUkpeU8OFVFVTqoSN06JhWVHa7B-iUESE7xhl7eC8_Qee1XpN2JNOC6sfohBOiaM_6U_RzFWco4HEFV2AOOeGtndtTqtgmjx3EiH_YduUy2RR29sBxdqmtaH2DY64V5xF_zv4NHpfkDnhIeL4CPIZoN5DmvNQ9NrWwqlsoU4ix5Sn4JdpUn6BHo40Vzm_jGfr67u2Xiw_d5af3Hy9Wl52TlM6dI9Rp4oTiinnn5Fop8NYPg5Zaac6BMHCWEb_mvZAcpGdMjL1kijunB8fP0Ouj7nZZb8C71lmx0WxL2NhyY7IN5m8khSsz5e9GESUFVU3gxa1Ayd8WqLPZhLpfkU3QZjSMDGQQRAysUZ__Q73OS0ltvMbqteZSyb0gO7JcaXssMN41Q4nZ-2yOPpvmszn4bHat6Nn9Me5KfrvaCPxIqA1KE5Q_f_9H9he2e7bW</recordid><startdate>20180730</startdate><enddate>20180730</enddate><creator>Boppidi, Karthik R.</creator><creator>Ribeiro, Liliane Fraga Costa</creator><creator>Iambamrung, Sirasa</creator><creator>Nelson, Sidney M.</creator><creator>Wang, Yan</creator><creator>Momany, Michelle</creator><creator>Richardson, Elizabeth A.</creator><creator>Lincoln, Stephen</creator><creator>Srivastava, Ranjan</creator><creator>Harris, Steven D.</creator><creator>Marten, Mark R.</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-4309-605X</orcidid></search><sort><creationdate>20180730</creationdate><title>Altered secretion patterns and cell wall organization caused by loss of PodB function in the filamentous fungus Aspergillus nidulans</title><author>Boppidi, Karthik R. ; Ribeiro, Liliane Fraga Costa ; Iambamrung, Sirasa ; Nelson, Sidney M. ; Wang, Yan ; Momany, Michelle ; Richardson, Elizabeth A. ; Lincoln, Stephen ; Srivastava, Ranjan ; Harris, Steven D. ; Marten, Mark R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c511t-c01c90c46362dcc5b66edad889596933e02eca20db37453e5d224f75263cc98c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>14/28</topic><topic>14/34</topic><topic>14/63</topic><topic>38/23</topic><topic>38/39</topic><topic>631/326/193/2096</topic><topic>631/61/252</topic><topic>82/58</topic><topic>Aspergillus nidulans</topic><topic>Aspergillus nidulans - cytology</topic><topic>Aspergillus nidulans - genetics</topic><topic>Aspergillus nidulans - growth & development</topic><topic>Aspergillus nidulans - metabolism</topic><topic>Cell Wall - metabolism</topic><topic>Cell Wall - ultrastructure</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Fungi</topic><topic>Gene Expression Regulation, Fungal</topic><topic>Genotype</topic><topic>Golgi cells</topic><topic>Humanities and Social Sciences</topic><topic>Hyphae - ultrastructure</topic><topic>multidisciplinary</topic><topic>Mutation</topic><topic>Mutation - genetics</topic><topic>Phenotype</topic><topic>Polarity</topic><topic>Protein folding</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>Relative abundance</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Secretion</topic><topic>Secretome</topic><topic>Temperature</topic><topic>Unfolded Protein Response</topic><topic>Up-Regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Boppidi, Karthik R.</creatorcontrib><creatorcontrib>Ribeiro, Liliane Fraga Costa</creatorcontrib><creatorcontrib>Iambamrung, Sirasa</creatorcontrib><creatorcontrib>Nelson, Sidney M.</creatorcontrib><creatorcontrib>Wang, Yan</creatorcontrib><creatorcontrib>Momany, Michelle</creatorcontrib><creatorcontrib>Richardson, Elizabeth A.</creatorcontrib><creatorcontrib>Lincoln, Stephen</creatorcontrib><creatorcontrib>Srivastava, Ranjan</creatorcontrib><creatorcontrib>Harris, Steven D.</creatorcontrib><creatorcontrib>Marten, Mark R.</creatorcontrib><collection>Springer Nature OA Free Journals</collection><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>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 SciTech 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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Boppidi, Karthik R.</au><au>Ribeiro, Liliane Fraga Costa</au><au>Iambamrung, Sirasa</au><au>Nelson, Sidney M.</au><au>Wang, Yan</au><au>Momany, Michelle</au><au>Richardson, Elizabeth A.</au><au>Lincoln, Stephen</au><au>Srivastava, Ranjan</au><au>Harris, Steven D.</au><au>Marten, Mark R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Altered secretion patterns and cell wall organization caused by loss of PodB function in the filamentous fungus Aspergillus nidulans</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2018-07-30</date><risdate>2018</risdate><volume>8</volume><issue>1</issue><spage>11433</spage><epage>11</epage><pages>11433-11</pages><artnum>11433</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Filamentous fungi are widely used in the production of a variety of industrially relevant enzymes and proteins as they have the unique ability to secrete tremendous amounts of proteins. However, the secretory pathways in filamentous fungi are not completely understood. Here, we investigated the role of a mutation in the POlarity Defective (
podB
) gene on growth, protein secretion, and cell wall organization in
Aspergillus nidulans
using a temperature sensitive (Ts) mutant. At restrictive temperature, the mutation resulted in lack of biomass accumulation, but led to a significant increase in specific protein productivity. Proteomic analysis of the secretome showed that the relative abundance of 584 (out of 747 identified) proteins was altered due to the mutation. Of these, 517 were secreted at higher levels. Other phenotypic differences observed in the mutant include up-regulation of unfolded protein response (UPR), deformation of Golgi apparatus and uneven cell wall thickness. Furthermore, proteomic analysis of cell wall components in the mutant revealed the presence of intracellular proteins in higher abundance accompanied by lower levels of most cell wall proteins. Taken together, results from this study suggest the importance of PodB as a target when engineering fungal strains for enhanced secretion of valuable biomolecules.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>30061727</pmid><doi>10.1038/s41598-018-29615-z</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0003-4309-605X</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Scientific reports, 2018-07, Vol.8 (1), p.11433-11, Article 11433 |
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| subjects | 14/28 14/34 14/63 38/23 38/39 631/326/193/2096 631/61/252 82/58 Aspergillus nidulans Aspergillus nidulans - cytology Aspergillus nidulans - genetics Aspergillus nidulans - growth & development Aspergillus nidulans - metabolism Cell Wall - metabolism Cell Wall - ultrastructure Fungal Proteins - genetics Fungal Proteins - metabolism Fungi Gene Expression Regulation, Fungal Genotype Golgi cells Humanities and Social Sciences Hyphae - ultrastructure multidisciplinary Mutation Mutation - genetics Phenotype Polarity Protein folding Proteins Proteomics Relative abundance Science Science (multidisciplinary) Secretion Secretome Temperature Unfolded Protein Response Up-Regulation |
| title | Altered secretion patterns and cell wall organization caused by loss of PodB function in the filamentous fungus Aspergillus nidulans |
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