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Analysing the contribution of nucleic acids to the structure and properties of centric heterochromatin

AuthorsCortés, Alfred; Huertas, Dori; Marsellach, Francesc Xavier ; Ferrer-Miralles, Neus; Ortiz-Lombardía, Miguel; Fanti, Laura; Pimpinelli, Sergio; Piña, Benjamín ; Azorín, Ferran
Satellite DNA
Multi-KH-domain proteins
Centromeric heterochromatin
DNA structure
Issue DateMar-2003
PublisherKluwer Academic Publishers
CitationGenetica 117(2-3): 117-125 (2003)
AbstractA class of repetitive DNA sequences frequently found at centromeric regions are R/Y-satellites showing an asymmetric distribution of residues resulting in one strand being rich in purines (R-strand) while the complementary strand is pyrimidine-rich (Y-strand). The dodeca-satellite of Drosophila belongs to this class of centromeric satellites. In vivo, the dodeca-satellite forms altered DNA structures in which the R-strand forms very stable intramolecular fold-backs that are stabilised by the formation of tandem G·A mismatches. A single-stranded nucleic acids binding protein, DDP1, binds the unstructured dodeca-satellite Y-strand with high affinity. In polytene chromosomes, DDP1 associates with the heterochromatic chromocenter and, at the euchromatic chromosome arms, co-localises with HP1. DDP1 is a vigilin. Vigilins are highly conserved multi-KH-domain proteins. Scp160p, the vigilin from S. cerevisiae, is involved in the control of ploidy. DDP1 complements a Δscp160 deletion.
Publisher version (URL)http://dx.doi.org/10.1023/A:1022947921402
Identifiersdoi: 10.1023/A:1022947921402
issn: 0016-6707
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