Purification and properties of the F sex factor TraD protein, an inner membrane conjugal transfer protein
Using a traD overexpression plasmid, we purified the F sex factor TraD protein in milligram quantities. The purified protein has an apparent molecular weight of 82,000 and an amino acid composition rich in acidic residues. Using specific antibodies, TraD was localized to the inner membrane of F+ cel...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-06, Vol.267 (18), p.12761-12766 |
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| container_end_page | 12766 |
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| container_issue | 18 |
| container_start_page | 12761 |
| container_title | The Journal of biological chemistry |
| container_volume | 267 |
| creator | M M Panicker E G Minkley, Jr |
| description | Using a traD overexpression plasmid, we purified the F sex factor TraD protein in milligram quantities. The purified protein
has an apparent molecular weight of 82,000 and an amino acid composition rich in acidic residues. Using specific antibodies,
TraD was localized to the inner membrane of F+ cells under conditions where it is produced in physiologically normal amounts.
Furthermore, the protein was soluble only in the presence of detergents, but there is evidence that the carboxyl terminus
is water-soluble. The purified protein shows pH-sensitive binding to DNA cellulose columns. |
| doi_str_mv | 10.1016/S0021-9258(18)42341-1 |
| format | Article |
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has an apparent molecular weight of 82,000 and an amino acid composition rich in acidic residues. Using specific antibodies,
TraD was localized to the inner membrane of F+ cells under conditions where it is produced in physiologically normal amounts.
Furthermore, the protein was soluble only in the presence of detergents, but there is evidence that the carboxyl terminus
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has an apparent molecular weight of 82,000 and an amino acid composition rich in acidic residues. Using specific antibodies,
TraD was localized to the inner membrane of F+ cells under conditions where it is produced in physiologically normal amounts.
Furthermore, the protein was soluble only in the presence of detergents, but there is evidence that the carboxyl terminus
is water-soluble. The purified protein shows pH-sensitive binding to DNA cellulose columns.</description><subject>Amino Acids - analysis</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding and carrier proteins</subject><subject>Biological and medical sciences</subject><subject>characterization</subject><subject>Chromatography, Affinity</subject><subject>Cloning, Molecular</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - isolation & purification</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins</subject><subject>F Factor</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Intracellular Membranes - metabolism</subject><subject>Isoelectric Focusing</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Weight</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>purification</subject><subject>TraD protein</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV1LHTEQhoMoemr9CUIuiljo2kw-NruXorUVBIVa8C5ksxNPZD9Ok11a_705noNempshzPPmncxLyDGwM2BQfv_NGIei5qo6heqr5EJCATtkAawShVDwsEsWb8gB-ZTSE8tH1rBP9qGESut6QcLdHIMPzk5hHKgdWrqK4wrjFDDR0dNpifSKJvxPvXXTGOl9tJdrZsIwfMsCGoYBI-2xb6IdkLpxeJofbUenfE0-t7bwZ7LnbZfwaFsPyZ-rH_cXv4qb25_XF-c3hZOSTQXWygvdoG9bKwRaXjFQ2GoohXDaW-3z52XjsFWMe8dVXerS-VowJVqe6yE52bybff_OmCbTh-Sw6_J045yMFkyWUskPwexYQ8VZBtUGdHFMKaI3qxh6G58NMLPOwrxmYdaLNlCZ1ywMZN3x1mBuemzfVZvl5_6Xbd8mZzufF-ZCesOUVABMvmPL8Lj8FyKaJoxuib3hpV77AdcliBcgo53u</recordid><startdate>19920625</startdate><enddate>19920625</enddate><creator>M M Panicker</creator><creator>E G Minkley, Jr</creator><general>American Society for Biochemistry and Molecular Biology</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19920625</creationdate><title>Purification and properties of the F sex factor TraD protein, an inner membrane conjugal transfer protein</title><author>M M Panicker ; E G Minkley, Jr</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-e95f37befdda33ea28015ed71633c7fa7f0164bced502fc259676cf93053d2f93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acids - analysis</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacterial Proteins - metabolism</topic><topic>Binding and carrier proteins</topic><topic>Biological and medical sciences</topic><topic>characterization</topic><topic>Chromatography, Affinity</topic><topic>Cloning, Molecular</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - isolation & purification</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Escherichia coli</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins</topic><topic>F Factor</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Intracellular Membranes - metabolism</topic><topic>Isoelectric Focusing</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Weight</topic><topic>Plasmids</topic><topic>Proteins</topic><topic>purification</topic><topic>TraD protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>M M Panicker</creatorcontrib><creatorcontrib>E G Minkley, Jr</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</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>M M Panicker</au><au>E G Minkley, Jr</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and properties of the F sex factor TraD protein, an inner membrane conjugal transfer protein</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-06-25</date><risdate>1992</risdate><volume>267</volume><issue>18</issue><spage>12761</spage><epage>12766</epage><pages>12761-12766</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Using a traD overexpression plasmid, we purified the F sex factor TraD protein in milligram quantities. The purified protein
has an apparent molecular weight of 82,000 and an amino acid composition rich in acidic residues. Using specific antibodies,
TraD was localized to the inner membrane of F+ cells under conditions where it is produced in physiologically normal amounts.
Furthermore, the protein was soluble only in the presence of detergents, but there is evidence that the carboxyl terminus
is water-soluble. The purified protein shows pH-sensitive binding to DNA cellulose columns.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1618779</pmid><doi>10.1016/S0021-9258(18)42341-1</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1992-06, Vol.267 (18), p.12761-12766 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73046454 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acids - analysis Analytical, structural and metabolic biochemistry Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Binding and carrier proteins Biological and medical sciences characterization Chromatography, Affinity Cloning, Molecular DNA-Binding Proteins - chemistry DNA-Binding Proteins - isolation & purification DNA-Binding Proteins - metabolism Electrophoresis, Polyacrylamide Gel Escherichia coli Escherichia coli - metabolism Escherichia coli Proteins F Factor Fundamental and applied biological sciences. Psychology Intracellular Membranes - metabolism Isoelectric Focusing Membrane Proteins - chemistry Membrane Proteins - isolation & purification Membrane Proteins - metabolism Molecular Weight Plasmids Proteins purification TraD protein |
| title | Purification and properties of the F sex factor TraD protein, an inner membrane conjugal transfer protein |
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