Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.3.1.28 (chloramphenicol acetyltransferase)
 5,100 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

From a mouse genomic DNA library we have isolated sequences containing the entire coding region for histone H1(0) mRNA, flanked by several kb at both the 3' and 5' ends. Deletions of the 5' upstream region ligated to the chloramphenicol acetyltransferase (CAT)-encoding gene as a reporter, have shown that a region from bp -400 to -600 is necessary and sufficient for efficient transcription. We have also shown that treatment of F9 teratocarcinoma cells with retinoic acid and cyclic AMP (which differentiates F9 cells to parietal endoderm) clearly increases CAT activity several times over the level found in untreated F9 cells. This increase was observed in transient, as well as in stably transfected cells. Analysis of the deletions in differentiating cells indicates that the element responsible for the observed increase in CAT activity, is contained within the first 700 bp upstream from the H1(0) mRNA cap site.
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PMID:Cloning and characterization of the mouse histone H1(0) promoter region. 280 18

It has been shown that the mouse histone H10 promoter contains a DNA element, composed of a direct repeat of the sequence GGTGACC separated by 7 nt, which is able to bind retinoic acid receptors and to modulate transcription of reporter genes following treatment with retinoic acid. We have now investigated whether this DNA motif is also responsive to thyroid hormone. We co-transfected CV-1 monkey kidney cells with chloramphenicol acetyltransferase (CAT) expression plasmids containing either 740 bp of the H10 wild-type promoter or five copies of the repeat element cloned in front of the thymidine kinase promoter and expression vectors for human thyroid hormone receptors (TRs) alpha or beta and retinoid X receptor alpha (RXR alpha). Treatment of transfected cells with triiodothyronine led to a dose-dependent increase in CAT activity. Transfection experiments with increasing amounts of expression vectors for either TR alpha or RXR alpha resulted in up to 6-fold enhancement of CAT transcription. Furthermore, point mutations within the half-sites of the response element of the H10 promoter, as well as deletions within the interspace region, lowered CAT activity to 60-80% of that of the wild-type control. Electrophoretic mobility shift assays showed that the repeat element was able to form retarded complexes with TR alpha homodimers, as well as with TR alpha-RXR alpha heterodimers. Our results suggest that thyroid hormone receptors are involved in the regulation of mouse histone H10 expression.
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PMID:Thyroid hormone receptors bind to the promoter of the mouse histone H10 gene and modulate its transcription. 855 62