Dimerization by colicin E3 in the absence of immunity protein
Using small angle x-ray scattering from solutions of colicin E3-immunity protein complex and the separated proteins, we have measured the radii of gyration of each species. We find that the complex is an elongated molecule with a radius of gyration of 35.5 +/- 0.7 A. Immunity protein is more compact...
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| Veröffentlicht in: | The Journal of biological chemistry 1983-09, Vol.258 (18), p.10967-10972 |
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| container_end_page | 10972 |
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| container_title | The Journal of biological chemistry |
| container_volume | 258 |
| creator | Levinson, B L Pickover, C A Richards, F M |
| description | Using small angle x-ray scattering from solutions of colicin E3-immunity protein complex and the separated proteins, we have measured the radii of gyration of each species. We find that the complex is an elongated molecule with a radius of gyration of 35.5 +/- 0.7 A. Immunity protein is more compact with a radius of gyration of 13.4 +/- 0.1 A. Upon removal of immunity protein from the complex, colicin E3 (form minus immunity protein) undergoes further elongation and dimerizes, such that its radius of gyration increases to 75.6 +/- 3.1 A. Dimerization is not reversed by simple addition of a stoichiometric amount of immunity protein to the E3 solution, even though this is sufficient to block in vitro activity. We suggest that the elongation, and perhaps dimer formation, occurs in vivo, concomitant with membrane translocation. |
| doi_str_mv | 10.1016/S0021-9258(17)44372-9 |
| format | Article |
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We find that the complex is an elongated molecule with a radius of gyration of 35.5 +/- 0.7 A. Immunity protein is more compact with a radius of gyration of 13.4 +/- 0.1 A. Upon removal of immunity protein from the complex, colicin E3 (form minus immunity protein) undergoes further elongation and dimerizes, such that its radius of gyration increases to 75.6 +/- 3.1 A. Dimerization is not reversed by simple addition of a stoichiometric amount of immunity protein to the E3 solution, even though this is sufficient to block in vitro activity. 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We find that the complex is an elongated molecule with a radius of gyration of 35.5 +/- 0.7 A. Immunity protein is more compact with a radius of gyration of 13.4 +/- 0.1 A. Upon removal of immunity protein from the complex, colicin E3 (form minus immunity protein) undergoes further elongation and dimerizes, such that its radius of gyration increases to 75.6 +/- 3.1 A. Dimerization is not reversed by simple addition of a stoichiometric amount of immunity protein to the E3 solution, even though this is sufficient to block in vitro activity. We suggest that the elongation, and perhaps dimer formation, occurs in vivo, concomitant with membrane translocation.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Bacterial Proteins</subject><subject>Biological and medical sciences</subject><subject>Colicins</subject><subject>Escherichia coli</subject><subject>Escherichia coli Proteins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Macromolecular Substances</subject><subject>Miscellaneous</subject><subject>Proteins</subject><subject>Scattering, Radiation</subject><subject>X-Rays</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkElrHDEQhUWIcSaT_ARDH0xwDu1o6dZyCMZ4iQOGHJJAbkJdU52p0Ist9cRMfr01C-NjRCEV1Ht6xcfYieDnggv96TvnUpRO1vZMmI9VpYws3Ss2E9yqUtXi12s2O0jesLcp_eH5VE4cs2Otai6dm7HP19RjpH9honEomnUBY0dAQ3GjinxPSyxCk3AALMa2oL5fDTSti4c4TkjDO3bUhi7h-_07Zz9vb35c3ZX33758vbq8L0FZ7spaG2WxcdzWBmRlGoEocieAV0aClq3QHMDoehGCNbZVSqMAaHkluFOo5uzD7t-c-7jCNPmeEmDXhQHHVfKWa6l0TpmzeieEOKYUsfUPkfoQ115wv8Hmt9j8hokXxm-xeZd9J_uAVdPj4uDac8rz0_08JAhdG8MAlA4yVykntX2RLen38oki-oZGWGLvt3m5uNtuebGTYWb2lzD6BLRhvMgWmPxipP_s-wyImZML</recordid><startdate>19830925</startdate><enddate>19830925</enddate><creator>Levinson, B L</creator><creator>Pickover, C A</creator><creator>Richards, F M</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>19830925</creationdate><title>Dimerization by colicin E3 in the absence of immunity protein</title><author>Levinson, B L ; Pickover, C A ; Richards, F M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3809-56738eb90857c247b1ee17c21c0472c62f160cc765daa878f336e1ccf041093e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Bacterial Proteins</topic><topic>Biological and medical sciences</topic><topic>Colicins</topic><topic>Escherichia coli</topic><topic>Escherichia coli Proteins</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Macromolecular Substances</topic><topic>Miscellaneous</topic><topic>Proteins</topic><topic>Scattering, Radiation</topic><topic>X-Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Levinson, B L</creatorcontrib><creatorcontrib>Pickover, C A</creatorcontrib><creatorcontrib>Richards, F M</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Levinson, B L</au><au>Pickover, C A</au><au>Richards, F M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dimerization by colicin E3 in the absence of immunity protein</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1983-09-25</date><risdate>1983</risdate><volume>258</volume><issue>18</issue><spage>10967</spage><epage>10972</epage><pages>10967-10972</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Using small angle x-ray scattering from solutions of colicin E3-immunity protein complex and the separated proteins, we have measured the radii of gyration of each species. We find that the complex is an elongated molecule with a radius of gyration of 35.5 +/- 0.7 A. Immunity protein is more compact with a radius of gyration of 13.4 +/- 0.1 A. Upon removal of immunity protein from the complex, colicin E3 (form minus immunity protein) undergoes further elongation and dimerizes, such that its radius of gyration increases to 75.6 +/- 3.1 A. Dimerization is not reversed by simple addition of a stoichiometric amount of immunity protein to the E3 solution, even though this is sufficient to block in vitro activity. We suggest that the elongation, and perhaps dimer formation, occurs in vivo, concomitant with membrane translocation.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>6350299</pmid><doi>10.1016/S0021-9258(17)44372-9</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1983-09, Vol.258 (18), p.10967-10972 |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Analytical, structural and metabolic biochemistry Bacterial Proteins Biological and medical sciences Colicins Escherichia coli Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Macromolecular Substances Miscellaneous Proteins Scattering, Radiation X-Rays |
| title | Dimerization by colicin E3 in the absence of immunity protein |
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