Purification and Characterization of Two Initiation Factors Required for Maximal Activity of a Highly Fractionated Globin mRNA Translation System
Two additional initiation factors (IF-M4 and IF-M5) have been purified and characterized both physically and biologically. IF-M4 is active as a single polypeptide chain with a molecular weight of 48,000. In contrast, IF-M5 is active as a complex with a molecular weight of about 500,000 and consists...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1976-08, Vol.73 (8), p.2584-2588 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Safer, Brian Adams, Sherrill L. Kemper, Wayne M. Berry, Karen W. Lloyd, Michele Merrick, William C. |
| description | Two additional initiation factors (IF-M4 and IF-M5) have been purified and characterized both physically and biologically. IF-M4 is active as a single polypeptide chain with a molecular weight of 48,000. In contrast, IF-M5 is active as a complex with a molecular weight of about 500,000 and consists of seven major and several minor polypeptide components. Analysis of IF-M5 in two polyacrylamide gel electrophoresis systems indicated that one of the major polypeptide chains of IF-M5 was the 35,000 dalton subunit of IF-MP. This analysis also revealed that IF-M2A, IF-M3, and elongation factor 2 were present as minor components. Both IF-M4 and IF-M5 are required to achieve maximal activity in an assay system dependent on exogenous globin mRNA, but neither factor has been observed to stimulate model reactions that utilize artificial templates [poly(U) or AUG]. |
| doi_str_mv | 10.1073/pnas.73.8.2584 |
| format | Article |
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IF-M4 is active as a single polypeptide chain with a molecular weight of 48,000. In contrast, IF-M5 is active as a complex with a molecular weight of about 500,000 and consists of seven major and several minor polypeptide components. Analysis of IF-M5 in two polyacrylamide gel electrophoresis systems indicated that one of the major polypeptide chains of IF-M5 was the 35,000 dalton subunit of IF-MP. This analysis also revealed that IF-M2A, IF-M3, and elongation factor 2 were present as minor components. Both IF-M4 and IF-M5 are required to achieve maximal activity in an assay system dependent on exogenous globin mRNA, but neither factor has been observed to stimulate model reactions that utilize artificial templates [poly(U) or AUG].</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.73.8.2584</identifier><identifier>PMID: 1066667</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Animals ; Cell-Free System ; Chromatography ; Coffee mugs ; Electrophoresis ; Gels ; Globins ; Messenger RNA ; Molecular Weight ; Peptide elongation factors ; Peptide Elongation Factors - analysis ; Peptide initiation factors ; Peptide Initiation Factors - analysis ; Peptide Initiation Factors - isolation & purification ; Poly U - metabolism ; Protein Biosynthesis ; Rabbits ; Reticulocytes ; Ribonucleoproteins - analysis ; Ribosomes ; RNA, Messenger - metabolism</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1976-08, Vol.73 (8), p.2584-2588</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4664-1421dce8570fc5bafd11691006a456451009740ddf31ad9bc14fa843017f33eb3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/73/8.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/66008$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/66008$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,728,781,785,804,886,27928,27929,53795,53797,58021,58254</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1066667$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Safer, Brian</creatorcontrib><creatorcontrib>Adams, Sherrill L.</creatorcontrib><creatorcontrib>Kemper, Wayne M.</creatorcontrib><creatorcontrib>Berry, Karen W.</creatorcontrib><creatorcontrib>Lloyd, Michele</creatorcontrib><creatorcontrib>Merrick, William C.</creatorcontrib><title>Purification and Characterization of Two Initiation Factors Required for Maximal Activity of a Highly Fractionated Globin mRNA Translation System</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Two additional initiation factors (IF-M4 and IF-M5) have been purified and characterized both physically and biologically. IF-M4 is active as a single polypeptide chain with a molecular weight of 48,000. In contrast, IF-M5 is active as a complex with a molecular weight of about 500,000 and consists of seven major and several minor polypeptide components. Analysis of IF-M5 in two polyacrylamide gel electrophoresis systems indicated that one of the major polypeptide chains of IF-M5 was the 35,000 dalton subunit of IF-MP. This analysis also revealed that IF-M2A, IF-M3, and elongation factor 2 were present as minor components. Both IF-M4 and IF-M5 are required to achieve maximal activity in an assay system dependent on exogenous globin mRNA, but neither factor has been observed to stimulate model reactions that utilize artificial templates [poly(U) or AUG].</description><subject>Animals</subject><subject>Cell-Free System</subject><subject>Chromatography</subject><subject>Coffee mugs</subject><subject>Electrophoresis</subject><subject>Gels</subject><subject>Globins</subject><subject>Messenger RNA</subject><subject>Molecular Weight</subject><subject>Peptide elongation factors</subject><subject>Peptide Elongation Factors - analysis</subject><subject>Peptide initiation factors</subject><subject>Peptide Initiation Factors - analysis</subject><subject>Peptide Initiation Factors - isolation & purification</subject><subject>Poly U - metabolism</subject><subject>Protein Biosynthesis</subject><subject>Rabbits</subject><subject>Reticulocytes</subject><subject>Ribonucleoproteins - analysis</subject><subject>Ribosomes</subject><subject>RNA, Messenger - metabolism</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1u3CAUha2qVTpNu-2iUiVW2dm92BibRRejUSaJlP4ona4RtiFDhM0EcJrJW-SNi-s0mm7KBnTPdw6gkyTvMWQYquLTbhA-q4qszvKyJi-SBQaGU0oYvEwWAHmV1iQnr5M33t8AACtrOEqOMNC4qkXy-H10WulWBG0HJIYOrbbCiTZIpx_moVVo88uii0EHPU_WUbfOoyt5O2onO6SsQ1_Eve6FQcs26Dsd9pNPoHN9vTV7tJ4io1WESJ8Z2-gB9Vdfl2jjxODNHPtj74Ps3yavlDBevnvaj5Of69PN6jy9_HZ2sVpepi2hlKSY5LhrZV1WoNqyEarDmDIMQAUpKSnjiVUEuk4VWHSsaTFRoiYF4EoVhWyK4-TznLsbm17GqCE4YfjOxV-4PbdC83-VQW_5tb3jMYOyPPpPnvzO3o7SB95r30pjxCDt6HldEEYZsAhmM9g6672T6vkODHzqkE8d8rjXfOowGj4evuwA_1PagT75_qqH_pP_6VyNxgR5HyL4YQZvfOzzmaQUoC5-A4wfu-k</recordid><startdate>19760801</startdate><enddate>19760801</enddate><creator>Safer, Brian</creator><creator>Adams, Sherrill L.</creator><creator>Kemper, Wayne M.</creator><creator>Berry, Karen W.</creator><creator>Lloyd, Michele</creator><creator>Merrick, William C.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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><scope>5PM</scope></search><sort><creationdate>19760801</creationdate><title>Purification and Characterization of Two Initiation Factors Required for Maximal Activity of a Highly Fractionated Globin mRNA Translation System</title><author>Safer, Brian ; Adams, Sherrill L. ; Kemper, Wayne M. ; Berry, Karen W. ; Lloyd, Michele ; Merrick, William C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4664-1421dce8570fc5bafd11691006a456451009740ddf31ad9bc14fa843017f33eb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Animals</topic><topic>Cell-Free System</topic><topic>Chromatography</topic><topic>Coffee mugs</topic><topic>Electrophoresis</topic><topic>Gels</topic><topic>Globins</topic><topic>Messenger RNA</topic><topic>Molecular Weight</topic><topic>Peptide elongation factors</topic><topic>Peptide Elongation Factors - analysis</topic><topic>Peptide initiation factors</topic><topic>Peptide Initiation Factors - analysis</topic><topic>Peptide Initiation Factors - isolation & purification</topic><topic>Poly U - metabolism</topic><topic>Protein Biosynthesis</topic><topic>Rabbits</topic><topic>Reticulocytes</topic><topic>Ribonucleoproteins - analysis</topic><topic>Ribosomes</topic><topic>RNA, Messenger - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Safer, Brian</creatorcontrib><creatorcontrib>Adams, Sherrill L.</creatorcontrib><creatorcontrib>Kemper, Wayne M.</creatorcontrib><creatorcontrib>Berry, Karen W.</creatorcontrib><creatorcontrib>Lloyd, Michele</creatorcontrib><creatorcontrib>Merrick, William C.</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Safer, Brian</au><au>Adams, Sherrill L.</au><au>Kemper, Wayne M.</au><au>Berry, Karen W.</au><au>Lloyd, Michele</au><au>Merrick, William C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Characterization of Two Initiation Factors Required for Maximal Activity of a Highly Fractionated Globin mRNA Translation System</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1976-08-01</date><risdate>1976</risdate><volume>73</volume><issue>8</issue><spage>2584</spage><epage>2588</epage><pages>2584-2588</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Two additional initiation factors (IF-M4 and IF-M5) have been purified and characterized both physically and biologically. IF-M4 is active as a single polypeptide chain with a molecular weight of 48,000. In contrast, IF-M5 is active as a complex with a molecular weight of about 500,000 and consists of seven major and several minor polypeptide components. Analysis of IF-M5 in two polyacrylamide gel electrophoresis systems indicated that one of the major polypeptide chains of IF-M5 was the 35,000 dalton subunit of IF-MP. This analysis also revealed that IF-M2A, IF-M3, and elongation factor 2 were present as minor components. Both IF-M4 and IF-M5 are required to achieve maximal activity in an assay system dependent on exogenous globin mRNA, but neither factor has been observed to stimulate model reactions that utilize artificial templates [poly(U) or AUG].</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>1066667</pmid><doi>10.1073/pnas.73.8.2584</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1976-08, Vol.73 (8), p.2584-2588 |
| issn | 0027-8424 1091-6490 |
| language | eng |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Animals Cell-Free System Chromatography Coffee mugs Electrophoresis Gels Globins Messenger RNA Molecular Weight Peptide elongation factors Peptide Elongation Factors - analysis Peptide initiation factors Peptide Initiation Factors - analysis Peptide Initiation Factors - isolation & purification Poly U - metabolism Protein Biosynthesis Rabbits Reticulocytes Ribonucleoproteins - analysis Ribosomes RNA, Messenger - metabolism |
| title | Purification and Characterization of Two Initiation Factors Required for Maximal Activity of a Highly Fractionated Globin mRNA Translation System |
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