Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
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Target Concepts:
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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)
Phosphoglycerate kinase (PGK), a
glycolytic enzyme
, possesses two isozymes: somatic-type PGK-1 and testis-specific PGK-2, encoded by distinct genes. Tissue-specific expression of the two PGK-encoding genes (Pgk) seems to be transcriptionally controlled, since tissue distribution of the mRNAs coincides well with that of the proteins. In the present study, we determined the cis-acting DNA elements that regulate the transcription of mouse Pgk-2. A transient expression assay of DNAs having various portions of the Pgk-2 upstream region linked to the
chloramphenicol acetyltransferase
(
CAT
)-encoding gene (cat) was performed using mouse cell lines that exclusively express Pgk-1. A substantial increase in cat expression was observed when the region between nucleotides (nt) -1404 and -685, relative to the most distal transcription start point at nt +1, was lost. This cis-acting region appeared to function as a silencer, since it repressed cat expression independently of either orientation to or distance from the Pgk-2 promoter. Moreover, the cis element inhibited Pgk-2 transcription with no effect on Pgk-1 transcription in a cell-free system using nuclear extracts of rat liver. These results suggest that a silencer-like negative cis element is responsible, at least partly, for tissue-specific transcription of Pgk-2.
...
PMID:A silencer-like cis element for the testis-specific phosphoglycerate-kinase-2-encoding gene. 139 12
The rat aldolase C gene encodes a
glycolytic enzyme
strongly expressed in adult brain. We previously reported that a 115-base pair (bp) promoter fragment was able to ensure the brain-specific expression of the
chloramphenicol acetyltransferase
(
CAT
) reporter gene in transgenic mice, but only at a low level (Thomas, M., Makeh, I., Briand, P., Kahn, A., and Skala, H. (1993) Eur. J. Biochem. 218, 143-151). Here we show that in vivo activation of this promoter at a high level requires cooperation between an upstream 0.6-kilobase pair (kb) fragment and far upstream sequences. In the 0.6-kb region, a 28-bp DNA element is shown to include overlapping in vitro binding sites for POU domain regulatory proteins and for the Winged Helix hepatocyte nuclear factor-3beta factor. An hepatocyte nuclear factor-3beta-binding site previously described in the short proximal promoter fragment is also shown to interact in vitro with POU proteins, although with a lower affinity than the 28-bp motif. Additional binding sites for POU factors were detected in the upstream 0.6-kb sequences. Progressive deletion in this region resulted in decreased expression levels of the transgenes in mice, suggesting synergistic interactions between these multiple POU-binding sites. We propose that DNA elements characterized by a dual binding specificity for both POU domain and Winged Helix transcription factors could play an essential role in the brain-specific expression of the aldolase C gene and other neuronal genes.
...
PMID:Upstream elements involved in vivo in activation of the brain-specific rat aldolase C gene. Role of binding sites for POU and winged helix proteins. 982 47
The rat aldolase C gene encodes a
glycolytic enzyme
strongly expressed in adult brain. We previously reported that a combination of distal and proximal 5' flanking sequences, the A + C + 0.8 kilobase (kb) pairs fragments, ensured high brain-specific expression in vivo (Skala et al. 1998). We show here that the expression pattern conferred by these sequences, when placed in front of the
chloramphenicol acetyltransferase
(
CAT
) or the enhanced green fluorescent protein (EGFP) reporter genes in transgenic mice, is similar to the distribution of the endogenous mRNA and protein. Double immunostaining for neuronal or glial cell-specific markers and for the EGFP protein indicates that the A + C + 0.8 kb genomic sequences from the rat aldolase C gene direct a predominant expression in neuronal cells of adult brain.
...
PMID:Neuronal expression of enhanced green fluorescent protein directed by 5' flanking sequences of the rat aldolase C gene in transgenic mice. 1471 81