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Amino acid sequence of honeybee prepromelittin synthesized in vitro
Translation of melittin messenger RNA from queen bee venom glands in a cell-free system from wheat germ yielded prepromelittin. Sequence analysis of the labeled in vitro product was performed by automatic Edman degradation of the intact polypeptide as well as by analysis of some of its proteolytic f...
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Published in: | Proceedings of the National Academy of Sciences - PNAS 1978-02, Vol.75 (2), p.701-704 |
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container_title | Proceedings of the National Academy of Sciences - PNAS |
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creator | Suchanek, G Kreil, G Hermodson, M.A |
description | Translation of melittin messenger RNA from queen bee venom glands in a cell-free system from wheat germ yielded prepromelittin. Sequence analysis of the labeled in vitro product was performed by automatic Edman degradation of the intact polypeptide as well as by analysis of some of its proteolytic fragments. Prepromelittin was shown to be composed of 70 amino acids, two of which have not been identified. The sequence of melittin is located in the COOH-terminal third of the polypeptide chain (residues 44-69). Prepromelittin starts with a very hydrophobic pre-region, probably 21 residues long, followed by a pro-part of unusual sequence, containing only alanine, proline, and acidic residues. At least three post-translational reactions are required to convert prepromelittin to melittin. |
doi_str_mv | 10.1073/pnas.75.2.701 |
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Sequence analysis of the labeled in vitro product was performed by automatic Edman degradation of the intact polypeptide as well as by analysis of some of its proteolytic fragments. Prepromelittin was shown to be composed of 70 amino acids, two of which have not been identified. The sequence of melittin is located in the COOH-terminal third of the polypeptide chain (residues 44-69). Prepromelittin starts with a very hydrophobic pre-region, probably 21 residues long, followed by a pro-part of unusual sequence, containing only alanine, proline, and acidic residues. 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Sequence analysis of the labeled in vitro product was performed by automatic Edman degradation of the intact polypeptide as well as by analysis of some of its proteolytic fragments. Prepromelittin was shown to be composed of 70 amino acids, two of which have not been identified. The sequence of melittin is located in the COOH-terminal third of the polypeptide chain (residues 44-69). Prepromelittin starts with a very hydrophobic pre-region, probably 21 residues long, followed by a pro-part of unusual sequence, containing only alanine, proline, and acidic residues. At least three post-translational reactions are required to convert prepromelittin to melittin.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animal glands</subject><subject>Apis mellifera</subject><subject>Bee Venoms - metabolism</subject><subject>Bees</subject><subject>Biochemistry</subject><subject>Cell free system</subject><subject>Electrophoresis</subject><subject>In Vitro Techniques</subject><subject>Material degradation</subject><subject>Melitten - metabolism</subject><subject>Messenger RNA</subject><subject>Neutral amino acids</subject><subject>Protein Biosynthesis</subject><subject>Protein Precursors - biosynthesis</subject><subject>RNA</subject><subject>Venoms</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><recordid>eNptkEtv1DAUhS3Eaygs2SAksoFdpn7FiRddVKMWKlViQbu2bM9Nx1ViB9tTMfx6PMp0VKSurKvvnOtzD0IfCV4S3LLTyeu0bJslXbaYvEALgiWpBZf4JVpgTNu645S_Re9SuscYy6bDb9Br2jLK6AKtzkfnQ6WtW1cJfm_BW6hCX22Ch50BqKYIUwwjDC5n56u083kDyf2FdVXGB5djeI9e9XpI8OHwnqDby4ub1Y_6-uf3q9X5dW1ZVyIBkdIaLnrbCKy56BinYJjQBXeNWcuGcwDWUwnSENlLoanmrBOGy9YYy07Q2bx32poR1hZ8jnpQU3SjjjsVtFP_E-826i48KE4Io7z4vx38MZRLU1ajSxaGQXsI26S6ElM0WBRhPQttDClF6I9_EKz2nat956ptFFWl86L__DTYUT2XXPDXA967HuGjW_XbYcjwJz9Z85yu4E8zvk85xCMXbdfsb_syw14Hpe-iS-r2Fy0uTGhHymHsHy8pp98</recordid><startdate>19780201</startdate><enddate>19780201</enddate><creator>Suchanek, G</creator><creator>Kreil, G</creator><creator>Hermodson, M.A</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>FBQ</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19780201</creationdate><title>Amino acid sequence of honeybee prepromelittin synthesized in vitro</title><author>Suchanek, G ; Kreil, G ; Hermodson, M.A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3891-e199cb46fc560a468342eb36ac3885bd9544ee3f29e9b19f96a2a4386b497bbc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animal glands</topic><topic>Apis mellifera</topic><topic>Bee Venoms - metabolism</topic><topic>Bees</topic><topic>Biochemistry</topic><topic>Cell free system</topic><topic>Electrophoresis</topic><topic>In Vitro Techniques</topic><topic>Material degradation</topic><topic>Melitten - metabolism</topic><topic>Messenger RNA</topic><topic>Neutral amino acids</topic><topic>Protein Biosynthesis</topic><topic>Protein Precursors - biosynthesis</topic><topic>RNA</topic><topic>Venoms</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Suchanek, G</creatorcontrib><creatorcontrib>Kreil, G</creatorcontrib><creatorcontrib>Hermodson, M.A</creatorcontrib><collection>AGRIS</collection><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>Suchanek, G</au><au>Kreil, G</au><au>Hermodson, M.A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amino acid sequence of honeybee prepromelittin synthesized in vitro</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1978-02-01</date><risdate>1978</risdate><volume>75</volume><issue>2</issue><spage>701</spage><epage>704</epage><pages>701-704</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Translation of melittin messenger RNA from queen bee venom glands in a cell-free system from wheat germ yielded prepromelittin. Sequence analysis of the labeled in vitro product was performed by automatic Edman degradation of the intact polypeptide as well as by analysis of some of its proteolytic fragments. Prepromelittin was shown to be composed of 70 amino acids, two of which have not been identified. The sequence of melittin is located in the COOH-terminal third of the polypeptide chain (residues 44-69). Prepromelittin starts with a very hydrophobic pre-region, probably 21 residues long, followed by a pro-part of unusual sequence, containing only alanine, proline, and acidic residues. At least three post-translational reactions are required to convert prepromelittin to melittin.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>273232</pmid><doi>10.1073/pnas.75.2.701</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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language | eng |
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source | JSTOR Archival Journals and Primary Sources Collection; PubMed Central |
subjects | Amino Acid Sequence Amino acids Animal glands Apis mellifera Bee Venoms - metabolism Bees Biochemistry Cell free system Electrophoresis In Vitro Techniques Material degradation Melitten - metabolism Messenger RNA Neutral amino acids Protein Biosynthesis Protein Precursors - biosynthesis RNA Venoms |
title | Amino acid sequence of honeybee prepromelittin synthesized in vitro |
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