ZF5, Which Is a Kruppel-Type Transcriptional Repressor, Requires the Zinc Finger Domain for Self-Association

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 imm...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1999-03, Vol.256 (3), p.573-578
Main Authors: Numoto, Michitaka, Yokoro, Ken, Koshi, Junko
Format: Article
Language:English
Subjects:
3T3 Cells
Animals
Binding Sites
Blotting, Western
Dimerization
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Gene Expression Regulation
Herpes simplex virus
HIV-1 - genetics
Human immunodeficiency virus
Kruppel-Like Transcription Factors
Mice
Promoter Regions, Genetic - genetics
Protein Binding
Protein Biosynthesis
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - metabolism
Repressor Proteins - chemistry
Repressor Proteins - genetics
Repressor Proteins - metabolism
Sequence Deletion
Simplexvirus - genetics
Thymidine Kinase - genetics
Trans-Activators - chemistry
Trans-Activators - metabolism
Transcription Factors - chemistry
Transfection
Zinc Fingers - genetics
Zinc Fingers - physiology
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1999.0375