| pubmed-article:14526028 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14526028 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:14526028 | lifeskim:mentions | umls-concept:C0597295 | lld:lifeskim |
| pubmed-article:14526028 | lifeskim:mentions | umls-concept:C0814810 | lld:lifeskim |
| pubmed-article:14526028 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
| pubmed-article:14526028 | lifeskim:mentions | umls-concept:C2003903 | lld:lifeskim |
| pubmed-article:14526028 | lifeskim:mentions | umls-concept:C1261552 | lld:lifeskim |
| pubmed-article:14526028 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:14526028 | pubmed:dateCreated | 2003-10-3 | lld:pubmed |
| pubmed-article:14526028 | pubmed:abstractText | Escherichia coli responses to four inhibitors that interfere with translation were monitored at the transcriptional level. A DNA microarray method provided a comprehensive view of changes in mRNA levels after exposure to these agents. Real-time reverse transcriptase PCRanalysis served to verify observations made with microarrays, and a chromosomal grpE::lux operon fusion was employed to specifically monitor the heat shock response. 4-Azaleucine, a competitive inhibitor of leucyl-tRNA synthetase, surprisingly triggered the heat shock response. Administration of mupirocin, an inhibitor of isoleucyl-tRNA synthetase activity, resulted in changes reminiscent of the stringent response. Treatment with kasugamycin and puromycin (targeting ribosomal subunit association as well as its peptidyl-transferase activity) caused accumulation of mRNAs from ribosomal protein operons. Abundant biosynthetic transcripts were often significantly diminished after treatment with any of these agents. Exposure of a relA strain to mupirocin resulted in accumulation of ribosomal protein operon transcripts. However, the relA strain's response to the other inhibitors was quite similar to that of the wild-type strain. | lld:pubmed |
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| pubmed-article:14526028 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:14526028 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14526028 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14526028 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:14526028 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:14526028 | pubmed:author | pubmed-author:SmulskiDana... | lld:pubmed |
| pubmed-article:14526028 | pubmed:author | pubmed-author:LaRossaRobert... | lld:pubmed |
| pubmed-article:14526028 | pubmed:author | pubmed-author:SöllDieterD | lld:pubmed |
| pubmed-article:14526028 | pubmed:author | pubmed-author:TempletonLori... | lld:pubmed |
| pubmed-article:14526028 | pubmed:author | pubmed-author:SabinaJeffrey... | lld:pubmed |
| pubmed-article:14526028 | pubmed:author | pubmed-author:DoverNirN | lld:pubmed |
| pubmed-article:14526028 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14526028 | pubmed:volume | 185 | lld:pubmed |
| pubmed-article:14526028 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14526028 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14526028 | pubmed:pagination | 6158-70 | lld:pubmed |
| pubmed-article:14526028 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:14526028 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14526028 | pubmed:articleTitle | Interfering with different steps of protein synthesis explored by transcriptional profiling of Escherichia coli K-12. | lld:pubmed |
| pubmed-article:14526028 | pubmed:affiliation | Central Research and Development, DuPont Company, Wilmington, Delaware 19880-0173, USA | lld:pubmed |
| pubmed-article:14526028 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14526028 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14526028 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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