| pubmed-article:8617219 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8617219 | lifeskim:mentions | umls-concept:C0031299 | lld:lifeskim |
| pubmed-article:8617219 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:8617219 | lifeskim:mentions | umls-concept:C0052605 | lld:lifeskim |
| pubmed-article:8617219 | lifeskim:mentions | umls-concept:C1336789 | lld:lifeskim |
| pubmed-article:8617219 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:8617219 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8617219 | pubmed:dateCreated | 1996-6-13 | lld:pubmed |
| pubmed-article:8617219 | pubmed:abstractText | Bacteriophage Mu repressor, which is stable in its wildtype form, can mutate to become sensitive to its Escherichia coli host ATP-dependent ClpXP protease. We further investigated the determinants of the mutant repressor's sensitivity to Clp. We show the crucial importance of a C-terminal, seven amino acid long sequence in which a single change is sufficient to decrease the rate of degradation of the protein. The sequence was fused at the C-terminal end of the CcdB and CcdA proteins encoded by plasmid F. CcdB, which is naturally stable, was unaffected, while CcdA, which is normally degraded by the Lon protease, became a substrate for ClpXP while remaining a substrate for Lon. In agreement with the current hypothesis on the mechanism of recognition of their substrates by energy- dependent proteases, these results support the existence, on the substrate polypeptides, of separate motifs responsible for recognition and cleavage by the protease. | lld:pubmed |
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| pubmed-article:8617219 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8617219 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8617219 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8617219 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8617219 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:8617219 | pubmed:author | pubmed-author:ToussaintAA | lld:pubmed |
| pubmed-article:8617219 | pubmed:author | pubmed-author:DesmetLL | lld:pubmed |
| pubmed-article:8617219 | pubmed:author | pubmed-author:GeuskensVV | lld:pubmed |
| pubmed-article:8617219 | pubmed:author | pubmed-author:GrimaudRR | lld:pubmed |
| pubmed-article:8617219 | pubmed:author | pubmed-author:LaachouchJ... | lld:pubmed |
| pubmed-article:8617219 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8617219 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8617219 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:8617219 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8617219 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8617219 | pubmed:pagination | 437-44 | lld:pubmed |
| pubmed-article:8617219 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8617219 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8617219 | pubmed:articleTitle | Bacteriophage Mu repressor as a target for the Escherichia coli ATP-dependent Clp Protease. | lld:pubmed |
| pubmed-article:8617219 | pubmed:affiliation | Laboratorie de Génétique des Procaryotes, Université Libre de Bruxelles, Genese, Belgium. | lld:pubmed |
| pubmed-article:8617219 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8617219 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8617219 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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