Leader polypeptides encoded in the 5′-region of the encephalomyocarditis virus genome
The authors have attempted to show here that: the initiator amino acid sequences, as defined by the presence of formyl-methionyl residue, are contained in a precursor polypeptide, preA; upon a short treatment of preA with a preparation of EMC virus-specific protease, these initiator sequences are cl...
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| Veröffentlicht in: | FEBS letters 1982-05, Vol.141 (2), p.153-156 |
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| creator | Kazachkov, Yu.A. Chernovskaya, T.V. Siyanova, E.Yu Svitkin, Yu.V. Ugarova, T.Yu Agol, V.I. |
| description | The authors have attempted to show here that: the initiator amino acid sequences, as defined by the presence of formyl-methionyl residue, are contained in a precursor polypeptide, preA; upon a short treatment of preA with a preparation of EMC virus-specific protease, these initiator sequences are cleaved off and emerge in two low-M sub(r) closely-related polypeptides, p14 and p12; after the removal of p14 (p12), the remaining moiety of preA corresponds to the precursor of capsid proteins, polypeptide A; preA, p14 and p12 appear to share an N-terminal amino acid sequence. These data suggest that all 3 latter polypeptides are initiated at a common single site on the viral genome and that p14 (p12) should occupy the N-terminal position on the EMC virus polyprotein cleavage map followed by polypeptide A, a precursor of the capsid proteins. |
| doi_str_mv | 10.1016/0014-5793(82)80035-5 |
| format | Article |
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Chernovskaya, T.V. ; Siyanova, E.Yu ; Svitkin, Yu.V. ; Ugarova, T.Yu ; Agol, V.I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5285-253fefafc1b8f48d72b98cc2f2b0872a89f41c1ce24e3cad022a2fed097efc983</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Animals</topic><topic>Carcinoma, Krebs 2 - metabolism</topic><topic>encephalomyocarditis virus</topic><topic>Encephalomyocarditis virus - genetics</topic><topic>Genes, Viral</topic><topic>Mice</topic><topic>Peptide Fragments - analysis</topic><topic>Peptides - genetics</topic><topic>Protein Biosynthesis</topic><topic>RNA, Viral - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kazachkov, Yu.A.</creatorcontrib><creatorcontrib>Chernovskaya, T.V.</creatorcontrib><creatorcontrib>Siyanova, E.Yu</creatorcontrib><creatorcontrib>Svitkin, Yu.V.</creatorcontrib><creatorcontrib>Ugarova, T.Yu</creatorcontrib><creatorcontrib>Agol, V.I.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kazachkov, Yu.A.</au><au>Chernovskaya, T.V.</au><au>Siyanova, E.Yu</au><au>Svitkin, Yu.V.</au><au>Ugarova, T.Yu</au><au>Agol, V.I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Leader polypeptides encoded in the 5′-region of the encephalomyocarditis virus genome</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1982-05-17</date><risdate>1982</risdate><volume>141</volume><issue>2</issue><spage>153</spage><epage>156</epage><pages>153-156</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The authors have attempted to show here that: the initiator amino acid sequences, as defined by the presence of formyl-methionyl residue, are contained in a precursor polypeptide, preA; upon a short treatment of preA with a preparation of EMC virus-specific protease, these initiator sequences are cleaved off and emerge in two low-M sub(r) closely-related polypeptides, p14 and p12; after the removal of p14 (p12), the remaining moiety of preA corresponds to the precursor of capsid proteins, polypeptide A; preA, p14 and p12 appear to share an N-terminal amino acid sequence. These data suggest that all 3 latter polypeptides are initiated at a common single site on the viral genome and that p14 (p12) should occupy the N-terminal position on the EMC virus polyprotein cleavage map followed by polypeptide A, a precursor of the capsid proteins.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>6284551</pmid><doi>10.1016/0014-5793(82)80035-5</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | FEBS letters, 1982-05, Vol.141 (2), p.153-156 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_74129498 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Carcinoma, Krebs 2 - metabolism encephalomyocarditis virus Encephalomyocarditis virus - genetics Genes, Viral Mice Peptide Fragments - analysis Peptides - genetics Protein Biosynthesis RNA, Viral - genetics |
| title | Leader polypeptides encoded in the 5′-region of the encephalomyocarditis virus genome |
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