THE DNA-BINDING ACTIVITY AND THE DIMERIZATION ABILITY OF THE THYROID TRANSCRIPTION FACTOR-I ARE REDOX REGULATED

被引：85

作者：

ARNONE, MI ^{[1
]}

ZANNINI, M ^{[1
]}

DILAURO, R ^{[1
]}

机构：

[1] Staz Zool Anton Dohrn, I-81021 NAPLES, ITALY

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1995年 / 270卷 / 20期

关键词：

D O I：

10.1074/jbc.270.20.12048

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The DNA binding activity of the thyroid transcription factor-1 (TTF-1), a homeodomain-containing protein implicated in the control of thyroid- and lung-specific transcription, is controlled, in vitro, by the redox potential, Oxidation decreases TTF-1 DNA binding activity, which is fully restored upon exposure to reducing agents. The decrease in DNA binding activity is due to the formation of disulfide bond(s), formed between two specific cysteine residues located outside the TTF-1 homeodomain; hence, oxidation does not appear to directly hinder TTF-1/DNA contacts, Disulfide bond formation seems to stabilize preexisting, loosely associated, TTF-1 dimers, which, upon oxidation, proceed in the formation of specific, higher order oligomers.

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页码：12048 / 12055

页数：8

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