Animal cells and systems
- 제1권4호
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- Pages.647-651
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- 1997
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- 1976-8354(pISSN)
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- 2151-2485(eISSN)
A Proline- and Leucine-rich 19 Amino Acid Oligopeptide from FS1 Functions as a Transcriptional Repression Domain
- Cho, Yong-Seok (Department of Genetic Engineering, Hallym University) ;
- Baek. Gum-Hee (Department of Genetic Engineering, Hallym University) ;
- Yoon, Sang-Soon (Department of Genetic Engineering, Hallym University) ;
- Han, Dong-Uck (Department of Genetic Engineering, Hallym University) ;
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Han, Kyu-Hyung
(Department of Genetic Engineering, Hallym University)
- 발행 : 1997.12.01
초록
We have used a transient expression assay employing Drosophila S2 cells to study the transcriptional repression activity of a 27 amino acid residue-long repression domain FS1 which was generated by a frame-shift in a pair-rule gene, even-skipped of Drosophila melanogaster. In an attempt to define a minimal requirement for the repression activity, we constructed a series of truncation mutant forms of the FS1, fused to a heterologous GAL4 DNA-binding domain, and measured their activities. All of the mutant forms, including the GAL4-FS1 (5-23) which retains the smallest number (19) of amino acid residues of FS1, were found to repress an initiator, a minimal TATA-lacking promoter, in a GAL4-binding-site-dependent manner. These findings suggest that a 19 amino acid residue-long region, rich in proline and leucine residues, is a transcriptional repression domain and may interact with the general transcription machinery.
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