The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling

The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling
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DOI:
10.1006/jmbi.1998.2355
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发表时间:
1999-01-15
影响因子:
5.6
通讯作者:
Tucker, PA
Tucker, PA
中科院分区:
生物学2区
文献类型:
--
作者:
Agianian, B;Leonard, K;Tucker, PA

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果蝇GAGA因子特异性结合GAGAG序列,并在体外与核小体重塑因子协同重塑染色质。它由一个介导蛋白-蛋白相互作用的n端结构域(POZ/BTB)、一个包含dna结合结构域的中心区域和一个c端富含谷氨酰胺的区域组成。结果表明,富含谷氨酰胺的区域负责在体外形成纤维,根据其着色特性和CD光谱,可归类为淀粉样纤维。在纤维形成时观察到一个大的结构变化,可能导致β -薄片结构。含有中心区域的突变体,无论是单独的还是与富含谷氨酰胺的区域一起,在很大程度上缺乏二级结构,但它们特异性地与同源DNA结合,并能够在体外重塑染色质。因此,GAGA因子的n端结构域和c端富含谷氨酰胺的区域都不是体外染色质重塑所必需的。(C) 1999学术出版社。
The Drosophila GAGA factor binds specifically to the sequence GAGAG, and synergises with nucleosome remodelling factor to remodel chromatin in vitro. It consists of an N-terminal domain (POZ/BTB) which mediates protein-protein interactions, a central region which contains the DNA-binding domain, and a C-terminal glutamine-rich region. It is shown that the glutamine-rich region is responsible for the formation of fibres in vitro which, on the basis of their tinctorial properties and CD spectra, may be classified as amyloid fibres. A large structural change, probably resulting in beta-sheet structure, is observed upon fibre formation. Mutants containing the central region, either alone or together with the glutamine-rich region, are largely lacking in secondary structure but they bind specifically to the cognate DNA and are able to remodel chromatin in vitro. Consequently, neither the N-terminal domain nor the C-terminal glutamine-rich regions of the GAGA factor are necessary for chromatin remodelling in vitro. (C) 1999 Academic Press.