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Identification of the transcriptional repression domain of nuclear factor 1-A.

Abstract：

:We previously showed that nuclear factor 1-A (NF1-A) binds to the silencer elements in the glutathione transferase P (GST-P) gene, and the carboxy terminal region of NF1-A represses the transcription activity of human metallothionein IIA (hMTIIA) promoter. In this study, we identified a repression region which is divided into two 100 amino acid domains (RD1 and RD2). RD1 increased the repression activity of RD2 to the hMTIIA promoter activity. The NF1-A repression domain inhibited the promoter activities of not only the hMTIIA gene but also those of the GST-P and CCAAT/enhancer binding protein delta genes. RD1 and RD2 had abundant serine and glycine residues, and proline and serine residues, respectively. Whereas some repression domains identified previously are enriched with alanine, proline, or serine, and are associated with the general transcription factors, the NF1-A repression domains did not interact with transcription factor IIB, TATA-binding protein (TBP), or TBP-associated factors in vitro.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Osada S,Ikeda T,Xu M,Nishihara T,Imagawa M

doi

10.1006/bbrc.1997.7382

subject

Has Abstract

pub_date

1997-09-29 00:00:00

pages

744-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(97)97382-4

journal_volume

238

pub_type

杂志文章

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