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

Cysteine-rich intestinal protein (CRIP) is an intestinal Zn(2+)-binding protein containing a single copy of the double Zn(2+)-finger arrangement known as the LIM motif. CRIP is developmentally regulated and can be induced by glucocorticoid hormones during the early suckling period. In this report we show that CRIP mRNA levels are induced by dexamethasone in cultured rat intestinal epithelial cells (IEC-6). Analysis of the 2644 bp of the 5'-flanking region of the CRIP gene revealed that the CRIP promoter lacks classical CAAT and TATA boxes but contains GC-rich regions in the proximal end of the promoter that probably function in transcription initiation. In addition to binding sites for transcription factors such as Sp-1, AP-2, OCT and GATA-2, there are multiple glucocorticoid-response elements. CRIP promoter constructs fused to the chloramphenicol acetyltransferase reporter gene and transfected into IEC-6 cells confirmed glucocorticoid responsiveness and the presence of negative acting elements. Mobility-shift assays revealed the presence of nuclear factors that bind to the CRIP promoter as a result of dexamethasone treatment. These experiments provide the initial data required to explore further the regulation of this tissue-specific developmentally regulated Zn(2+)-finger protein.
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PMID:Cloning and initial characterization of the promoter region of the rat cysteine-rich intestinal protein gene. 798 Apr 39

The herpes simplex virus 1 (HSV-1) replicative cycle begins by binding of the viral activator, VP16, to a set of sequences in the immediate-early (IE) gene promoters. With the aim of inhibiting this cycle, we have constructed a number of synthetic zinc-finger DNA-binding peptides by using recently reported methods. Peptides containing either three or six fingers, targeted to a viral promoter, were engineered as fusions with a KOX-1 transcription repression domain. These proteins bound to the HSV-1 IE175k (ICP4) promoter, in vitro, with nanomolar or subnanomolar binding affinity. However, in a chloramphenicol acetyltransferase reporter system, only the six-finger protein was found to repress VP16-activated transcription significantly. Thus the longer array of zinc fingers is required to compete successfully against VP16, one of the most powerful natural activators known. We found that the HSV-1 replication cycle can be partially repressed by the six-finger peptide with the viral titer reduced by 90%.
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PMID:Inhibition of herpes simplex virus 1 gene expression by designer zinc-finger transcription factors. 1257 1