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A purification method for a molecular complex in which a scaffold molecule is fully loaded with heterogeneous molecules
An affinity resin-based pull-down method is convenient for the purification of biochemical materials. However, its use is difficult for the isolation of a molecular complex fully loaded with multiple components from a reaction mixture containing the starting materials and intermediate products. To o...
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| Published in: | PloS one 2015-03, Vol.10 (3), p.e0120576-e0120576 |
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| container_end_page | e0120576 |
| container_issue | 3 |
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| creator | Ohuchi, Shoji J Sagawa, Fumihiko Ohno, Hirohisa Inoue, Tan |
| description | An affinity resin-based pull-down method is convenient for the purification of biochemical materials. However, its use is difficult for the isolation of a molecular complex fully loaded with multiple components from a reaction mixture containing the starting materials and intermediate products. To overcome this problem, we have developed a new purification procedure that depends on sequential elimination of the residues. In practice, two affinity resins were used for purifying a triangular-shaped RNP (RNA-protein complex) consisting of three ribosomal proteins (L7Ae) bound to an RNA scaffold. First, a resin with immobilized L7Ae protein captured the incomplete RNP complexes and the free RNA scaffold. Next, another resin with an immobilized chemically modified RNA of a derivative of Box C/D motif, the binding partner of L7Ae, was used to capture free protein. The complete triangular RNP was successfully purified from the mixture by these two steps. Obviously, the purified triangular RNP displaying three protein-binding peptides exhibited an improved performance when compared with the unrefined product. Conceptually, this purification procedure should be applicable for the purification of a variety of complexes consisting of multiple components other than RNP. |
| doi_str_mv | 10.1371/journal.pone.0120576 |
| format | article |
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However, its use is difficult for the isolation of a molecular complex fully loaded with multiple components from a reaction mixture containing the starting materials and intermediate products. To overcome this problem, we have developed a new purification procedure that depends on sequential elimination of the residues. In practice, two affinity resins were used for purifying a triangular-shaped RNP (RNA-protein complex) consisting of three ribosomal proteins (L7Ae) bound to an RNA scaffold. First, a resin with immobilized L7Ae protein captured the incomplete RNP complexes and the free RNA scaffold. Next, another resin with an immobilized chemically modified RNA of a derivative of Box C/D motif, the binding partner of L7Ae, was used to capture free protein. The complete triangular RNP was successfully purified from the mixture by these two steps. Obviously, the purified triangular RNP displaying three protein-binding peptides exhibited an improved performance when compared with the unrefined product. Conceptually, this purification procedure should be applicable for the purification of a variety of complexes consisting of multiple components other than RNP.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0120576</identifier><identifier>PMID: 25781936</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Affinity ; Binding ; Deoxyribonucleic acid ; DNA ; Laboratories ; Ligands ; Methods ; Peptides ; Protein binding ; Proteins ; Purification ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Resins ; Ribonucleic acid ; Ribosomal proteins ; Ribosomal Proteins - chemistry ; Ribosomal Proteins - isolation & purification ; RNA ; RNA polymerase ; RNA, Ribosomal - chemistry ; RNA, Ribosomal - isolation & purification ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - isolation & purification</subject><ispartof>PloS one, 2015-03, Vol.10 (3), p.e0120576-e0120576</ispartof><rights>COPYRIGHT 2015 Public Library of Science</rights><rights>2015 Ohuchi et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2015 Ohuchi et al 2015 Ohuchi et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c802t-efd1fe8c7f82c373d432125bf7eeee4701c66353ce0d730228da92272e3ac4ed3</citedby><cites>FETCH-LOGICAL-c802t-efd1fe8c7f82c373d432125bf7eeee4701c66353ce0d730228da92272e3ac4ed3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1664222574/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1664222574?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25781936$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Chang, Ing-Feng</contributor><creatorcontrib>Ohuchi, Shoji J</creatorcontrib><creatorcontrib>Sagawa, Fumihiko</creatorcontrib><creatorcontrib>Ohno, Hirohisa</creatorcontrib><creatorcontrib>Inoue, Tan</creatorcontrib><title>A purification method for a molecular complex in which a scaffold molecule is fully loaded with heterogeneous molecules</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>An affinity resin-based pull-down method is convenient for the purification of biochemical materials. However, its use is difficult for the isolation of a molecular complex fully loaded with multiple components from a reaction mixture containing the starting materials and intermediate products. To overcome this problem, we have developed a new purification procedure that depends on sequential elimination of the residues. In practice, two affinity resins were used for purifying a triangular-shaped RNP (RNA-protein complex) consisting of three ribosomal proteins (L7Ae) bound to an RNA scaffold. First, a resin with immobilized L7Ae protein captured the incomplete RNP complexes and the free RNA scaffold. Next, another resin with an immobilized chemically modified RNA of a derivative of Box C/D motif, the binding partner of L7Ae, was used to capture free protein. The complete triangular RNP was successfully purified from the mixture by these two steps. Obviously, the purified triangular RNP displaying three protein-binding peptides exhibited an improved performance when compared with the unrefined product. Conceptually, this purification procedure should be applicable for the purification of a variety of complexes consisting of multiple components other than RNP.</description><subject>Affinity</subject><subject>Binding</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Laboratories</subject><subject>Ligands</subject><subject>Methods</subject><subject>Peptides</subject><subject>Protein binding</subject><subject>Proteins</subject><subject>Purification</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Resins</subject><subject>Ribonucleic acid</subject><subject>Ribosomal proteins</subject><subject>Ribosomal Proteins - chemistry</subject><subject>Ribosomal Proteins - isolation & purification</subject><subject>RNA</subject><subject>RNA polymerase</subject><subject>RNA, Ribosomal - chemistry</subject><subject>RNA, Ribosomal - isolation & purification</subject><subject>RNA-Binding Proteins - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ohuchi, Shoji J</au><au>Sagawa, Fumihiko</au><au>Ohno, Hirohisa</au><au>Inoue, Tan</au><au>Chang, Ing-Feng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A purification method for a molecular complex in which a scaffold molecule is fully loaded with heterogeneous molecules</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2015-03-17</date><risdate>2015</risdate><volume>10</volume><issue>3</issue><spage>e0120576</spage><epage>e0120576</epage><pages>e0120576-e0120576</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>An affinity resin-based pull-down method is convenient for the purification of biochemical materials. However, its use is difficult for the isolation of a molecular complex fully loaded with multiple components from a reaction mixture containing the starting materials and intermediate products. To overcome this problem, we have developed a new purification procedure that depends on sequential elimination of the residues. In practice, two affinity resins were used for purifying a triangular-shaped RNP (RNA-protein complex) consisting of three ribosomal proteins (L7Ae) bound to an RNA scaffold. First, a resin with immobilized L7Ae protein captured the incomplete RNP complexes and the free RNA scaffold. Next, another resin with an immobilized chemically modified RNA of a derivative of Box C/D motif, the binding partner of L7Ae, was used to capture free protein. The complete triangular RNP was successfully purified from the mixture by these two steps. Obviously, the purified triangular RNP displaying three protein-binding peptides exhibited an improved performance when compared with the unrefined product. Conceptually, this purification procedure should be applicable for the purification of a variety of complexes consisting of multiple components other than RNP.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>25781936</pmid><doi>10.1371/journal.pone.0120576</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Affinity Binding Deoxyribonucleic acid DNA Laboratories Ligands Methods Peptides Protein binding Proteins Purification Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Resins Ribonucleic acid Ribosomal proteins Ribosomal Proteins - chemistry Ribosomal Proteins - isolation & purification RNA RNA polymerase RNA, Ribosomal - chemistry RNA, Ribosomal - isolation & purification RNA-Binding Proteins - chemistry RNA-Binding Proteins - isolation & purification |
| title | A purification method for a molecular complex in which a scaffold molecule is fully loaded with heterogeneous molecules |
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