Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.1.21 (thymidine kinase)
 7,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have cloned a cDNA encoding a new murine C2H2 zinc finger protein, ZF5. The 51.3 kD protein contains five GL1-Kruppel type zinc fingers at the C-terminus. At its N-terminus, ZF5 has a 41 amino acid region which was found to be homologous to the N-termini of several other zinc finger proteins. This region defines a new motif within zinc finger proteins which we have named the Zinc finger N-terminal (ZiN) domain. ZF5 binds to two sites in the c-myc promoter and to the -50 bp site of the herpes simplex thymidine kinase promoter. ZF5 is a transcriptional repressor and its repression domain is located N-terminal to the zinc finger domains. A single 4 kb ZF5 mRNA is expressed widely.
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PMID:Transcriptional repressor ZF5 identifies a new conserved domain in zinc finger proteins. 836 94

ZF5, which we have cloned as a repressor on the mouse c-myc promoter, is a zinc finger protein containing Kruppel-type zinc finger and ZiN/POZ domains. In a reverse transcriptase PCR assay using mouse skeletal muscle RNA, we identified a 827 bp PCR product including the zinc finger domain of ZF5 and the acidic domain of VP16. The presence of the VP16 acidic domain induced the reduction of DNA-binding activity of the zinc finger domain. In addition, the inhibitory effect of the VP16 acidic domain was demonstrated on the human immunodeficiency virus (HIV) promoter, but there was no effect on the thymidine kinase (TK) promoter.
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PMID:Detection of mouse skeletal muscle-specific product, which includes ZF5 zinc fingers and a VP16 acidic domain, by reverse transcriptase PCR. 922 18

ZF5, which we have cloned as a transcriptional repressor on the mouse c-myc promoter, has the POZ domain at the amino-terminus and the Kruppel-type zinc finger domain at the carboxy-terminus. In this report, we showed that ZF5 has two contradictory functions in transcription: activation of human immunodeficiency virus (HIV) promoter and repression of the HSV thymidine kinase (TK) promoter. The POZ domain contributed to the repressor activity, whereas the active function resulted from the DNA-binding ability of the zinc finger domain. We demonstrated that the POZ domain has a function mediating homomeric protein-protein interaction and this interaction requires the zinc finger domain. Furthermore, the POZ domain decreased the DNA-binding activity of the zinc finger domain. These results can provide evidence indicating the important interaction between the POZ and zinc finger domains.
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PMID:ZF5, which is a Kruppel-type transcriptional repressor, requires the zinc finger domain for self-association. 1008 Sep 39