Abstract
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 β-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.
Original language | English (US) |
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Pages (from-to) | 527-544 |
Number of pages | 18 |
Journal | Journal of Molecular Biology |
Volume | 285 |
Issue number | 2 |
DOIs | |
State | Published - Jan 15 1999 |
Externally published | Yes |
Keywords
- Amyloid
- Chromatin remodelling
- Drosophila
- GAGA
- Glutamine-rich
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology