A novel fusion partner for enhanced secretion of recombinant proteins in Saccharomyces cerevisiae
Expressing proteins with fusion partners improves yield and simplifies the purification process. We developed a novel fusion partner to improve the secretion of heterologous proteins that are otherwise poorly excreted in yeast. The VOA1 (YGR106C) gene of Saccharomyces cerevisiae encodes a subunit of...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2016-12, Vol.100 (24), p.10453-10461 |
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| creator | Bae, Jung-Hoon Sung, Bong Hyun Seo, Jeong-Woo Kim, Chul Ho Sohn, Jung-Hoon |
| description | Expressing proteins with fusion partners improves yield and simplifies the purification process. We developed a novel fusion partner to improve the secretion of heterologous proteins that are otherwise poorly excreted in yeast. The
VOA1
(YGR106C) gene of
Saccharomyces cerevisiae
encodes a subunit of vacuolar ATPase. We found that C-terminally truncated Voa1p was highly secreted into the culture medium, even when fused with rarely secreted heterologous proteins such as human interleukin-2 (hIL-2). Deletion mapping of C-terminally truncated Voa1p, identified a hydrophilic 28-amino acid peptide (HL peptide) that was responsible for the enhanced secretion of target protein. A purification tag and a protease cleavage site were added to use HL peptide as a multi-purpose fusion partner. The utility of this system was tested via the expression and purification of various heterologous proteins. In many cases, the yield of target proteins fused with the peptide was significantly increased, and fusion proteins could be directly purified with affinity chromatography. The fusion partner was removed by in vitro processing, and intact proteins were purified by re-application of samples to affinity chromatography. |
| doi_str_mv | 10.1007/s00253-016-7722-2 |
| format | Article |
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VOA1
(YGR106C) gene of
Saccharomyces cerevisiae
encodes a subunit of vacuolar ATPase. We found that C-terminally truncated Voa1p was highly secreted into the culture medium, even when fused with rarely secreted heterologous proteins such as human interleukin-2 (hIL-2). Deletion mapping of C-terminally truncated Voa1p, identified a hydrophilic 28-amino acid peptide (HL peptide) that was responsible for the enhanced secretion of target protein. A purification tag and a protease cleavage site were added to use HL peptide as a multi-purpose fusion partner. The utility of this system was tested via the expression and purification of various heterologous proteins. In many cases, the yield of target proteins fused with the peptide was significantly increased, and fusion proteins could be directly purified with affinity chromatography. The fusion partner was removed by in vitro processing, and intact proteins were purified by re-application of samples to affinity chromatography.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-016-7722-2</identifier><identifier>PMID: 27412460</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>affinity chromatography ; Amino acids ; Biomedical and Life Sciences ; Biotechnologically Relevant Enzymes and Proteins ; Biotechnology ; Chromatography ; chromosome mapping ; Cloning ; culture media ; Cytokines ; Fermentation ; Gene expression ; genes ; Glucose ; H-transporting ATP synthase ; humans ; hydrophilicity ; interleukin-2 ; Interleukin-2 - genetics ; Interleukin-2 - secretion ; Life Sciences ; Microbial Genetics and Genomics ; Microbiology ; Peptides ; Physiological aspects ; Plasmids ; Protein Engineering - methods ; proteinases ; Proteins ; purification methods ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - secretion ; Recombinant proteins ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - secretion ; secretion ; Studies ; Vacuolar Proton-Translocating ATPases - genetics ; Vacuolar Proton-Translocating ATPases - secretion ; Yeast ; Yeasts</subject><ispartof>Applied microbiology and biotechnology, 2016-12, Vol.100 (24), p.10453-10461</ispartof><rights>The Author(s) 2016</rights><rights>COPYRIGHT 2016 Springer</rights><rights>Applied Microbiology and Biotechnology is a copyright of Springer, 2016.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c674t-34f9d12cb4a89332125aeb8e81c6f095a93039deaba02a0e4afdacf94353ee8c3</citedby><cites>FETCH-LOGICAL-c674t-34f9d12cb4a89332125aeb8e81c6f095a93039deaba02a0e4afdacf94353ee8c3</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/s00253-016-7722-2$$EPDF$$P50$$Gspringer$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-016-7722-2$$EHTML$$P50$$Gspringer$$Hfree_for_read</linktohtml><link.rule.ids>230,314,778,782,883,27907,27908,41471,42540,51302</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27412460$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bae, Jung-Hoon</creatorcontrib><creatorcontrib>Sung, Bong Hyun</creatorcontrib><creatorcontrib>Seo, Jeong-Woo</creatorcontrib><creatorcontrib>Kim, Chul Ho</creatorcontrib><creatorcontrib>Sohn, Jung-Hoon</creatorcontrib><title>A novel fusion partner for enhanced secretion of recombinant proteins in Saccharomyces cerevisiae</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>Expressing proteins with fusion partners improves yield and simplifies the purification process. We developed a novel fusion partner to improve the secretion of heterologous proteins that are otherwise poorly excreted in yeast. The
VOA1
(YGR106C) gene of
Saccharomyces cerevisiae
encodes a subunit of vacuolar ATPase. We found that C-terminally truncated Voa1p was highly secreted into the culture medium, even when fused with rarely secreted heterologous proteins such as human interleukin-2 (hIL-2). Deletion mapping of C-terminally truncated Voa1p, identified a hydrophilic 28-amino acid peptide (HL peptide) that was responsible for the enhanced secretion of target protein. A purification tag and a protease cleavage site were added to use HL peptide as a multi-purpose fusion partner. The utility of this system was tested via the expression and purification of various heterologous proteins. In many cases, the yield of target proteins fused with the peptide was significantly increased, and fusion proteins could be directly purified with affinity chromatography. The fusion partner was removed by in vitro processing, and intact proteins were purified by re-application of samples to affinity chromatography.</description><subject>affinity chromatography</subject><subject>Amino acids</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnologically Relevant Enzymes and Proteins</subject><subject>Biotechnology</subject><subject>Chromatography</subject><subject>chromosome mapping</subject><subject>Cloning</subject><subject>culture media</subject><subject>Cytokines</subject><subject>Fermentation</subject><subject>Gene expression</subject><subject>genes</subject><subject>Glucose</subject><subject>H-transporting ATP synthase</subject><subject>humans</subject><subject>hydrophilicity</subject><subject>interleukin-2</subject><subject>Interleukin-2 - genetics</subject><subject>Interleukin-2 - secretion</subject><subject>Life Sciences</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Peptides</subject><subject>Physiological aspects</subject><subject>Plasmids</subject><subject>Protein Engineering - methods</subject><subject>proteinases</subject><subject>Proteins</subject><subject>purification methods</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - secretion</subject><subject>Recombinant proteins</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - secretion</subject><subject>secretion</subject><subject>Studies</subject><subject>Vacuolar Proton-Translocating ATPases - genetics</subject><subject>Vacuolar Proton-Translocating ATPases - secretion</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</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>eNqNkl2L1DAUhoMo7jj6A7yRgDd60TVfbdobYVj8WFgQXL0OZ9LTmSxtMibt4P57U2dcdkRRchHIec6bnDcvIc85O-eM6TeJMVHKgvGq0FqIQjwgC66kKFjF1UOyYFyXhS6b-ow8SemGMS7qqnpMzoRWXKiKLQisqA977Gk3JRc83UEcPUbahUjRb8FbbGlCG3Gcy6GjEW0Y1s6DH-kuhhGdT9R5eg3WbiGG4dZiohYj7l1ygE_Jow76hM-O-5J8ff_uy8XH4urTh8uL1VVhK63GQqquabmwawV1I6XgogRc11hzW3WsKaGRTDYtwhqYAIYKuhZs1yhZSsTayiV5e9DdTesBW4t-jNCbXXQDxFsTwJnTindbswl7U3Le1EpkgVdHgRi-TZhGM7hkse_BY5iSEYwxVXNV1v9EeV0yrTlT-j9QUWnBtJIZffkbehOm6LNpmVJC8Ub_vPtIbaBH43wX8jR2FjUrpXl-pcimLMn5H6i8WhycDR47l89PGl6fNGRmxO_jBqaUzOX151OWH1gbQ0oRuzuXOTNzMs0hmSYn08zJNLO7L-5_z13HryhmQByAlEt-g_He9H9V_QFykuyq</recordid><startdate>20161201</startdate><enddate>20161201</enddate><creator>Bae, Jung-Hoon</creator><creator>Sung, Bong Hyun</creator><creator>Seo, Jeong-Woo</creator><creator>Kim, Chul Ho</creator><creator>Sohn, Jung-Hoon</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</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>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>7QO</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20161201</creationdate><title>A novel fusion partner for enhanced secretion of recombinant proteins in Saccharomyces cerevisiae</title><author>Bae, Jung-Hoon ; Sung, Bong Hyun ; Seo, Jeong-Woo ; Kim, Chul Ho ; Sohn, Jung-Hoon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c674t-34f9d12cb4a89332125aeb8e81c6f095a93039deaba02a0e4afdacf94353ee8c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>affinity chromatography</topic><topic>Amino acids</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnologically Relevant Enzymes and Proteins</topic><topic>Biotechnology</topic><topic>Chromatography</topic><topic>chromosome mapping</topic><topic>Cloning</topic><topic>culture media</topic><topic>Cytokines</topic><topic>Fermentation</topic><topic>Gene expression</topic><topic>genes</topic><topic>Glucose</topic><topic>H-transporting ATP synthase</topic><topic>humans</topic><topic>hydrophilicity</topic><topic>interleukin-2</topic><topic>Interleukin-2 - genetics</topic><topic>Interleukin-2 - secretion</topic><topic>Life Sciences</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Peptides</topic><topic>Physiological aspects</topic><topic>Plasmids</topic><topic>Protein Engineering - methods</topic><topic>proteinases</topic><topic>Proteins</topic><topic>purification methods</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - secretion</topic><topic>Recombinant proteins</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - secretion</topic><topic>secretion</topic><topic>Studies</topic><topic>Vacuolar Proton-Translocating ATPases - genetics</topic><topic>Vacuolar Proton-Translocating ATPases - secretion</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bae, Jung-Hoon</creatorcontrib><creatorcontrib>Sung, Bong Hyun</creatorcontrib><creatorcontrib>Seo, Jeong-Woo</creatorcontrib><creatorcontrib>Kim, Chul Ho</creatorcontrib><creatorcontrib>Sohn, Jung-Hoon</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>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>ABI/INFORM Collection</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</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 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>ABI/INFORM Collection (Alumni Edition)</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>Business Premium 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>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</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>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</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>Biotechnology Research Abstracts</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bae, Jung-Hoon</au><au>Sung, Bong Hyun</au><au>Seo, Jeong-Woo</au><au>Kim, Chul Ho</au><au>Sohn, Jung-Hoon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel fusion partner for enhanced secretion of recombinant proteins in Saccharomyces cerevisiae</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2016-12-01</date><risdate>2016</risdate><volume>100</volume><issue>24</issue><spage>10453</spage><epage>10461</epage><pages>10453-10461</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>Expressing proteins with fusion partners improves yield and simplifies the purification process. We developed a novel fusion partner to improve the secretion of heterologous proteins that are otherwise poorly excreted in yeast. The
VOA1
(YGR106C) gene of
Saccharomyces cerevisiae
encodes a subunit of vacuolar ATPase. We found that C-terminally truncated Voa1p was highly secreted into the culture medium, even when fused with rarely secreted heterologous proteins such as human interleukin-2 (hIL-2). Deletion mapping of C-terminally truncated Voa1p, identified a hydrophilic 28-amino acid peptide (HL peptide) that was responsible for the enhanced secretion of target protein. A purification tag and a protease cleavage site were added to use HL peptide as a multi-purpose fusion partner. The utility of this system was tested via the expression and purification of various heterologous proteins. In many cases, the yield of target proteins fused with the peptide was significantly increased, and fusion proteins could be directly purified with affinity chromatography. The fusion partner was removed by in vitro processing, and intact proteins were purified by re-application of samples to affinity chromatography.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>27412460</pmid><doi>10.1007/s00253-016-7722-2</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0175-7598 |
| ispartof | Applied microbiology and biotechnology, 2016-12, Vol.100 (24), p.10453-10461 |
| issn | 0175-7598 1432-0614 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5119842 |
| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | affinity chromatography Amino acids Biomedical and Life Sciences Biotechnologically Relevant Enzymes and Proteins Biotechnology Chromatography chromosome mapping Cloning culture media Cytokines Fermentation Gene expression genes Glucose H-transporting ATP synthase humans hydrophilicity interleukin-2 Interleukin-2 - genetics Interleukin-2 - secretion Life Sciences Microbial Genetics and Genomics Microbiology Peptides Physiological aspects Plasmids Protein Engineering - methods proteinases Proteins purification methods Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - secretion Recombinant proteins Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - secretion secretion Studies Vacuolar Proton-Translocating ATPases - genetics Vacuolar Proton-Translocating ATPases - secretion Yeast Yeasts |
| title | A novel fusion partner for enhanced secretion of recombinant proteins in Saccharomyces cerevisiae |
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