Morphogenesis of the long tail fibers of bacteriophage T2 involves proteolytic processing of the polypeptide (gene product 37) constituting the distal part of the fiber
Gene 37 of phage T2 codes for a protein that, as a dimer, constitutes the most distal, receptor-recognizing part of its long tail fibers. It was found that, from a plasmid carrying a fragment of gene 37 that lacked a region of the gene encoding 87 CO 2H-terminal amino acid residues, a protein was ex...
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Veröffentlicht in: | Journal of molecular biology 1986-09, Vol.191 (2), p.267-272 |
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creator | Drexler, Klaus Riede, Isolde Henning, Ulf |
description | Gene 37 of phage T2 codes for a protein that, as a dimer, constitutes the most distal, receptor-recognizing part of its long tail fibers. It was found that, from a plasmid carrying a fragment of gene 37 that lacked a region of the gene encoding 87 CO
2H-terminal amino acid residues, a protein was expressed that was slightly larger than that present in the phage. This size difference could not be accounted for. The missing region of gene 37 and also gene 38 (which codes for the auxiliary protein required for dimerization of protein 37) were cloned. Plasmids were constructed with gene 37, or gene 37 together with gene 38, under inducible control. Independent of the presence of the latter gene, a protein was produced that had the same size as protein 37 in the phage. A pulse-chase experiment revealed that a precursor of protein 37 is synthesized and processed such that approximately 120 amino acid residues, most likely CO
2H-terminal, are removed. Therefore, the protein produced from the truncated gene was larger because it cannot be processed. This fact also solved an old puzzle: an amber fragment of protein 37 of phage T2 had been found to be larger than the mature protein. The amber codon could be located 24 codons away from the normal stop codon. Obviously, the fragment cannot be processed. The existence of this fragment demonstrates that processing occurs during phage maturation. |
doi_str_mv | 10.1016/0022-2836(86)90263-9 |
format | Article |
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2H-terminal amino acid residues, a protein was expressed that was slightly larger than that present in the phage. This size difference could not be accounted for. The missing region of gene 37 and also gene 38 (which codes for the auxiliary protein required for dimerization of protein 37) were cloned. Plasmids were constructed with gene 37, or gene 37 together with gene 38, under inducible control. Independent of the presence of the latter gene, a protein was produced that had the same size as protein 37 in the phage. A pulse-chase experiment revealed that a precursor of protein 37 is synthesized and processed such that approximately 120 amino acid residues, most likely CO
2H-terminal, are removed. Therefore, the protein produced from the truncated gene was larger because it cannot be processed. This fact also solved an old puzzle: an amber fragment of protein 37 of phage T2 had been found to be larger than the mature protein. The amber codon could be located 24 codons away from the normal stop codon. Obviously, the fragment cannot be processed. The existence of this fragment demonstrates that processing occurs during phage maturation.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/0022-2836(86)90263-9</identifier><identifier>PMID: 3543378</identifier><identifier>CODEN: JMOBAK</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Autoradiography ; Biological and medical sciences ; Cloning, Molecular ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Microbiology ; Morphogenesis ; Mutation ; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains ; T-Phages - genetics ; T-Phages - physiology ; Transcription, Genetic ; Viral Proteins - metabolism ; Virology</subject><ispartof>Journal of molecular biology, 1986-09, Vol.191 (2), p.267-272</ispartof><rights>1986</rights><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-630dee3b143a8ec9827b44449003507dc3628b9a9612bec0459aced15621ad8a3</citedby><cites>FETCH-LOGICAL-c386t-630dee3b143a8ec9827b44449003507dc3628b9a9612bec0459aced15621ad8a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0022-2836(86)90263-9$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7879053$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3543378$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Drexler, Klaus</creatorcontrib><creatorcontrib>Riede, Isolde</creatorcontrib><creatorcontrib>Henning, Ulf</creatorcontrib><title>Morphogenesis of the long tail fibers of bacteriophage T2 involves proteolytic processing of the polypeptide (gene product 37) constituting the distal part of the fiber</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>Gene 37 of phage T2 codes for a protein that, as a dimer, constitutes the most distal, receptor-recognizing part of its long tail fibers. It was found that, from a plasmid carrying a fragment of gene 37 that lacked a region of the gene encoding 87 CO
2H-terminal amino acid residues, a protein was expressed that was slightly larger than that present in the phage. This size difference could not be accounted for. The missing region of gene 37 and also gene 38 (which codes for the auxiliary protein required for dimerization of protein 37) were cloned. Plasmids were constructed with gene 37, or gene 37 together with gene 38, under inducible control. Independent of the presence of the latter gene, a protein was produced that had the same size as protein 37 in the phage. A pulse-chase experiment revealed that a precursor of protein 37 is synthesized and processed such that approximately 120 amino acid residues, most likely CO
2H-terminal, are removed. Therefore, the protein produced from the truncated gene was larger because it cannot be processed. This fact also solved an old puzzle: an amber fragment of protein 37 of phage T2 had been found to be larger than the mature protein. The amber codon could be located 24 codons away from the normal stop codon. Obviously, the fragment cannot be processed. The existence of this fragment demonstrates that processing occurs during phage maturation.</description><subject>Autoradiography</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Microbiology</subject><subject>Morphogenesis</subject><subject>Mutation</subject><subject>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</subject><subject>T-Phages - genetics</subject><subject>T-Phages - physiology</subject><subject>Transcription, Genetic</subject><subject>Viral Proteins - metabolism</subject><subject>Virology</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1u1DAUhS0EKtPCG4DkBULtIuCfxLE3lVBFAamITVlbjn0zY5SJg-2M1DfiMXFmwizxxpbvd46v70HoDSUfKKHiIyGMVUxycS3FjSJM8Eo9QxtKpKqk4PI52pyRl-gypV-EkIbX8gJd8KbmvJUb9Od7iNMubGGE5BMOPc47wEMYtzgbP-DedxCP952xGaIP085sAT8y7MdDGA6Q8BRDhjA8ZW-Xs4WUfNGvXlOpTDBl7wBfL-8sjJttxry9wTaMKfs850Wx4M6nbAY8mZj_ORx7eIVe9GZI8Hrdr9DP-8-Pd1-rhx9fvt19eqgslyJXghMHwDtacyPBKsnari5LEcIb0jrLBZOdMkpQ1oEldaOMBUcbwahx0vAr9P7kW7r8PUPKeu-ThWEwI4Q56bZlQnHGC1ifQBtDShF6PUW_N_FJU6KXgPQyfb1MX0uhjwFpVWRvV_-524M7i9ZESv3dWjfJmqGPZrQ-nbFWtqqEWLDbEwZlFgcPUSfrYSxf8RFs1i74__fxF45gruw</recordid><startdate>19860920</startdate><enddate>19860920</enddate><creator>Drexler, Klaus</creator><creator>Riede, Isolde</creator><creator>Henning, Ulf</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</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></search><sort><creationdate>19860920</creationdate><title>Morphogenesis of the long tail fibers of bacteriophage T2 involves proteolytic processing of the polypeptide (gene product 37) constituting the distal part of the fiber</title><author>Drexler, Klaus ; Riede, Isolde ; Henning, Ulf</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-630dee3b143a8ec9827b44449003507dc3628b9a9612bec0459aced15621ad8a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Autoradiography</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Microbiology</topic><topic>Morphogenesis</topic><topic>Mutation</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>T-Phages - genetics</topic><topic>T-Phages - physiology</topic><topic>Transcription, Genetic</topic><topic>Viral Proteins - metabolism</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Drexler, Klaus</creatorcontrib><creatorcontrib>Riede, Isolde</creatorcontrib><creatorcontrib>Henning, Ulf</creatorcontrib><collection>Pascal-Francis</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><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Drexler, Klaus</au><au>Riede, Isolde</au><au>Henning, Ulf</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Morphogenesis of the long tail fibers of bacteriophage T2 involves proteolytic processing of the polypeptide (gene product 37) constituting the distal part of the fiber</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1986-09-20</date><risdate>1986</risdate><volume>191</volume><issue>2</issue><spage>267</spage><epage>272</epage><pages>267-272</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><coden>JMOBAK</coden><abstract>Gene 37 of phage T2 codes for a protein that, as a dimer, constitutes the most distal, receptor-recognizing part of its long tail fibers. It was found that, from a plasmid carrying a fragment of gene 37 that lacked a region of the gene encoding 87 CO
2H-terminal amino acid residues, a protein was expressed that was slightly larger than that present in the phage. This size difference could not be accounted for. The missing region of gene 37 and also gene 38 (which codes for the auxiliary protein required for dimerization of protein 37) were cloned. Plasmids were constructed with gene 37, or gene 37 together with gene 38, under inducible control. Independent of the presence of the latter gene, a protein was produced that had the same size as protein 37 in the phage. A pulse-chase experiment revealed that a precursor of protein 37 is synthesized and processed such that approximately 120 amino acid residues, most likely CO
2H-terminal, are removed. Therefore, the protein produced from the truncated gene was larger because it cannot be processed. This fact also solved an old puzzle: an amber fragment of protein 37 of phage T2 had been found to be larger than the mature protein. The amber codon could be located 24 codons away from the normal stop codon. Obviously, the fragment cannot be processed. The existence of this fragment demonstrates that processing occurs during phage maturation.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>3543378</pmid><doi>10.1016/0022-2836(86)90263-9</doi><tpages>6</tpages></addata></record> |
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subjects | Autoradiography Biological and medical sciences Cloning, Molecular Electrophoresis, Polyacrylamide Gel Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Microbiology Morphogenesis Mutation Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains T-Phages - genetics T-Phages - physiology Transcription, Genetic Viral Proteins - metabolism Virology |
title | Morphogenesis of the long tail fibers of bacteriophage T2 involves proteolytic processing of the polypeptide (gene product 37) constituting the distal part of the fiber |
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