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)

A 1,937 bp PstI-HindIII fragment containing the ipaR locus was cloned from the large invasion plasmid of Shigella dysenteriae CG097, and its nucleotide sequence was completely determined. The IpaR protein (35 kDa, calculated from the DNA sequence) was synthesized in Escherichia coli chi 1411 minicells containing the 1,937-bp PstI-HindIII fragment. To determine the regulatory role of ipaR for ipa genes, we applied genetic complementation experiments using chloramphenicol acetyltransferase (CAT) as reporter. Analyses of CAT activity of the recombinant plasmids containing the 5' flanking sequences of the 24-kDa-protein gene and the ippI, ipaB, ipaC, and ipaD genes defined strong promoters upstream of the 24-kDa-protein gene and ipaD gene, weak promoters upstream of the ippI and ipaB genes, and the absence of any promoter activity for the ipaC gene. Complementation analyses showed that the CAT activity only under direction of the ippI promoter region increased 1.8-fold in the presence of IpaR protein. On the basis of our data, we suggest that an operon comprising ippI, ipaB, and ipaC is positively regulated by IpaR protein which has a trans effect on a DNA sequence upstream of the ippI promoter.
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PMID:Nucleotide sequence and transcriptional regulation of a positive regulatory gene of Shigella dysenteriae. 154 32

The androgen receptor (AR) is a nuclear transcription factor that is essential for development of the male urogenital tract. In the current work, we have characterized the mouse androgen receptor suppressor (mARS). A single, 20-base pair, region (TCCCCCCACCCACCCCC-CCT) was sufficient for suppression in chloramphenicol acetyltransferase assays. Northern analysis indicated that translational regulation is not necessary for the suppression. Analysis of the AR mRNA half-life indicated that the mARS does not affect AR RNA degradation. Gel mobility assays showed that the mARS is bound by multiple proteins that can recognize single-stranded DNA and RNA. In addition, differing proteins are expressed in distinct tissues. Purification of some of these proteins has shown that a doublet of 33 and 35 kDa binds to the G-rich strand and that a 52-kDa protein binds to the C-rich strand. Southwestern blots have confirmed that these proteins are indeed recognized by the mARS. The results of these experiments indicate that the AR 5'-untranslated region contains a suppressor element that can be bound by multiple proteins. The mARS appears to be acting either by altering transcription initiation or blocking transcription elongation. Characterization of this suppressor may provide insight into the physiological means by which the AR is regulated.
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PMID:The androgen receptor is transcriptionally suppressed by proteins that bind single-stranded DNA. 773 38

Milk protein gene expression in mammary epithelial cells is regulated by interactions of the cells with each other and with extracellular-matrix components, and by the lactogenic hormones. Cell-cell and cell-extracellular-matrix interactions confer a state of competence to HC11 mammary epithelial cells. Cellular confluence and matrix deposition are prerequisites for the lactogenic hormone induction of, for example, beta-casein synthesis. We have studied how these cellular interactions influence transcription factor activity. Proximal and distal regulatory elements have been identified in the DNA of the beta-casein gene promoter that confer transcriptional induction to the lactogenic hormones in competent cells. A region located between positions -221 and -170 of the rat beta-casein promoter contains overlapping binding sites for DNA binding factors with positive and negative regulatory activity. A construct containing 221 nt of 5' promoter sequences linked to a chloramphenicol acetyltransferase (CAT) reporter gene and transfected into HC11 cells has low constitutive expression and is strongly inducible. Deletion of the sequences to -183 results in an increase in both constitutive and induced expression. Mutations in or deletion of the region from -183 to -170 abolish promoter activity. A sequence-specific single-stranded DNA binding transcriptional repressor (STR), composed of two proteins, binds to the upper strand of the -194 to -163 fragment and negatively regulates transcription. STR also recognizes the 5' untranslated region of the beta-casein mRNA and is sequestered into the cytoplasm by RNA after lactogenic hormone induction. Sequestration by RNA allows an activator to bind to the fragment -183 to -170. This activator has been identified as SARP, a sequence-specific single-stranded DNA activator region binding protein. The binding site of SARP is found both in the upper and the lower strands of this fragment. SARP has no affinity for RNA. It enhances transcription of a promoter construct containing rat beta-casein promoter sequences from -183 to -1 and of a heterologous promoter containing multimerized copies of the -194 to -163 fragment in a lactogenic-hormone-independent manner. Mutations between positions -183 and -170, which result in a loss of promoter activity, also prevent SARP from binding to the DNA. Confluence of HC11 cells up-regulates the DNA binding activity of SARP. High SARP activity is also detected in mammary gland cells of lactating mice and is regulated by suckling. Withdrawal of pups from their lactating mothers results in a rapid decrease of SARP activity. We have purified SARP from the lactating mammary tissue of sheep and have identified proteins of 28 and 35 kDa.
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PMID:Regulation of gene expression in mammary epithelial cells by cellular confluence and sequence-specific DNA binding factors. 951 16

The activity of a 35 kDa protease increased in response to induced expression of chloramphenicol acetyltransferase (CAT) in E. coli. This protease was partially purified, extensively characterized, and identified via the use of zymogram gels as the outer membrane protease, OmpT. In experiments targeting the overlap of well-characterized stress responses, OmpT activity was found to increase in response to heat shock but was only minimally affected by amino acid limitation. The largest increase in activity was found after induction of CAT. OmpT expression levels also increased in response to induction of recombinant CAT overexpression and heat shock. This is the first report of increased activity and expression of an outer membrane protease during cytoplasmic overexpression of a recombinant protein.
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PMID:OmpT expression and activity increase in response to recombinant chloramphenicol acetyltransferase overexpression and heat shock in E. coli. 1093 37