An improved method for the heterologous production of soluble human ribosomal proteins in Escherichia coli
Human ribosomal proteins play important structural and functional roles in the ribosome and in protein synthesis. An efficient method to recombinantly produce and purify these proteins would enable their full characterisation. However, the production of human ribosomal proteins can be challenging. T...
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| Veröffentlicht in: | Scientific reports 2019-06, Vol.9 (1), p.8884-8, Article 8884 |
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| description | Human ribosomal proteins play important structural and functional roles in the ribosome and in protein synthesis. An efficient method to recombinantly produce and purify these proteins would enable their full characterisation. However, the production of human ribosomal proteins can be challenging. The only published method about the recombinant production of human ribosomal proteins involved the recovery of proteins from inclusion bodies, a process that is tedious and may lead to significant loss of yield. Herein, we explored the use of different
Escherichia coli
competent cells and fusion protein tags for the recombinant production of human ribosomal proteins. We found that, by using thioredoxin as a fusion protein, soluble ribosomal protein could be obtained directly from cell lysates, thus leading to an improved method to recombinantly produce these proteins. |
| doi_str_mv | 10.1038/s41598-019-45323-8 |
| format | Article |
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Escherichia coli
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Escherichia coli
competent cells and fusion protein tags for the recombinant production of human ribosomal proteins. 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H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An improved method for the heterologous production of soluble human ribosomal proteins in Escherichia coli</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2019-06-20</date><risdate>2019</risdate><volume>9</volume><issue>1</issue><spage>8884</spage><epage>8</epage><pages>8884-8</pages><artnum>8884</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Human ribosomal proteins play important structural and functional roles in the ribosome and in protein synthesis. An efficient method to recombinantly produce and purify these proteins would enable their full characterisation. However, the production of human ribosomal proteins can be challenging. The only published method about the recombinant production of human ribosomal proteins involved the recovery of proteins from inclusion bodies, a process that is tedious and may lead to significant loss of yield. Herein, we explored the use of different
Escherichia coli
competent cells and fusion protein tags for the recombinant production of human ribosomal proteins. We found that, by using thioredoxin as a fusion protein, soluble ribosomal protein could be obtained directly from cell lysates, thus leading to an improved method to recombinantly produce these proteins.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>31222068</pmid><doi>10.1038/s41598-019-45323-8</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0003-2509-9521</orcidid><orcidid>https://orcid.org/0000-0001-7957-4530</orcidid><orcidid>https://orcid.org/0000-0003-0633-6771</orcidid><orcidid>https://orcid.org/0000-0003-4945-8904</orcidid><orcidid>https://orcid.org/0000-0002-6990-525X</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 631/1647 631/92 82/80 82/83 E coli Escherichia coli Escherichia coli - genetics Fusion protein Humanities and Social Sciences Humans Inclusion bodies Ions Lysates multidisciplinary Protein biosynthesis Protein synthesis Proteins Recombinant Proteins - metabolism Ribosomal proteins Ribosomal Proteins - biosynthesis Ribosomal Proteins - metabolism Science Science (multidisciplinary) Structure-function relationships Thioredoxin |
| title | An improved method for the heterologous production of soluble human ribosomal proteins in Escherichia coli |
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