| pubmed-article:3280550 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3280550 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:3280550 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:3280550 | lifeskim:mentions | umls-concept:C0205102 | lld:lifeskim |
| pubmed-article:3280550 | lifeskim:mentions | umls-concept:C1515333 | lld:lifeskim |
| pubmed-article:3280550 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:3280550 | lifeskim:mentions | umls-concept:C1527118 | lld:lifeskim |
| pubmed-article:3280550 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:3280550 | pubmed:dateCreated | 1988-5-12 | lld:pubmed |
| pubmed-article:3280550 | pubmed:abstractText | The inner membrane TET (TetA) protein, which is involved in Tn10-mediated microbial tetracycline resistance, consists of two domains, alpha and beta, both of which are needed for tetracycline resistance and efflux (M.S. Curiale, L.M. McMurry, and S.B. Levy, J. Bacteriol. 157:211-217, 1984). Since tetracycline-sensitive mutants in one domain can partially complement sensitive mutants in the other domain and since some sensitive mutants show dominance over the wild type, a multimeric structure for TET in the membrane had been suggested. We have studied this possibility by using tetA-phoA gene fusions. We fused all but the last 40 base pairs of the tetA gene with the carboxy terminus of the phoA gene for alkaline phosphatase (PhoA), whose activity requires its dimerization in the periplasm. The tetA-phoA fusion protein was under control of the tetracycline-inducible regulatory system for the tetA gene. Induction led to the synthesis of a 78,000-dalton inner membrane protein. Tetracycline resistance was expressed at reduced levels, consistent with the terminal beta domain deletion. Alkaline phosphatase activity was also present, but at low levels, suggesting that some, but not all, of the fusion proteins had their carboxy-terminal ends in the periplasm. When wild-type or mutant TET proteins were present in the same cell with the fusion protein, the tetracycline resistance level was affected (raised or lowered); however, phosphatase activity was reduced only when TET proteins with intact or near-intact beta domains were present. These findings suggest that TET functions as a multimer and that intact beta domains, on TET molecules in the heterologous multimer, either allow fewer PhoA moieties to project into the periplasm or sterically hinder PhoA moieties from dimerizing. | lld:pubmed |
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| pubmed-article:3280550 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3280550 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3280550 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3280550 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3280550 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:3280550 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:3280550 | pubmed:author | pubmed-author:LevyS BSB | lld:pubmed |
| pubmed-article:3280550 | pubmed:author | pubmed-author:HickmanR KRK | lld:pubmed |
| pubmed-article:3280550 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3280550 | pubmed:volume | 170 | lld:pubmed |
| pubmed-article:3280550 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3280550 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3280550 | pubmed:pagination | 1715-20 | lld:pubmed |
| pubmed-article:3280550 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:3280550 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3280550 | pubmed:articleTitle | Evidence that TET protein functions as a multimer in the inner membrane of Escherichia coli. | lld:pubmed |
| pubmed-article:3280550 | pubmed:affiliation | Department of Molecular Biology, Tufts University School of Medicine, Boston, Massachusetts 02111. | lld:pubmed |
| pubmed-article:3280550 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3280550 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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