ArticleMolecular and cellular biology2000
DDP1, a heterochromatin-associated multi-KH-domain protein of Drosophila melanogaster, interacts specifically with centromeric satellite DNA sequences.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 38 citations in OpenAlex.
- Vigilin protein Vgl1 is required for heterochromatin-mediated gene silencing inThe Journal of biological chemistry · 2019Article
- Position-effect variegation, heterochromatin formation, and gene silencing in Drosophila.Cold Spring Harbor perspectives in biology · 2013Review
- Vgl1, a multi-KH domain protein, is a novel component of the fission yeast stress granules required for cell survival under thermal stress.Nucleic acids research · 2010Article
- On the mechanism of induction of heterochromatin by the RNA-binding protein vigilin.RNA (New York, N.Y.) · 2008Article
- Molecular analysis of core kinetochore composition and assembly in Drosophila melanogaster.PloS one · 2007Article
- Functional overlap between conserved and diverged KH domains in Saccharomyces cerevisiae SCP160.Nucleic acids research · 2007Article
- Determination and augmentation of RNA sequence specificity of the Nova K-homology domains.Nucleic acids research · 2004Article
- Both KH and non-KH domain sequences are required for polyribosome association of Scp160p in yeast.Nucleic acids research · 2004Article
- Genetic and biochemical interactions between SCP160 and EAP1 in yeast.Nucleic acids research · 2003Article
- RNAi-mediated depletion of the 15 KH domain protein, vigilin, induces death of dividing and non-dividing human cells but does not initially inhibit protein synthesis.Nucleic acids research · 2003Article
- Scp160p associates with specific mRNAs in yeast.Nucleic acids research · 2003Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DDP1 is a single-stranded nucleic acid binding protein of Drosophila melanogaster that associates with pericentric heterochromatin. DDP1 contains 15 consecutive KH domains and is homologous to the highly conserved vigilin proteins that, in Saccharomyces cerevisiae, are involved in the control of cell ploidy. DDP1 was identified and purified on the basis of its binding to the pyrimidine-rich C strand of the centromeric Drosophila dodeca-satellite. Here, the interaction of DDP1 with the dodeca-satellite C strand was analyzed in detail. This interaction is sequence specific. In particular, a guanine residue which is highly conserved in natural dodeca-satellite sequences was found to be essential for the efficient binding of DDP1. DDP1 binding was also found to be strongly influenced by the length and extent of secondary structure of the DNA substrate. Efficient DDP1 binding required a minimal length of about 75 to 100 nucleotides and was facilitated by the lack of secondary structure of the substrate. DDP1 also showed a significant affinity for the unstructured pyrimidine-rich strand of the most abundant centromeric Drosophila AAGAG satellite. The stoichiometry of the complexes formed with the dodeca-satellite C strand suggests that, in DDP1, the 15 consecutive KH domains are organized such that they define two nucleic acid binding surfaces. These results are discussed in the context of the possible contribution of DDP1 to heterochromatin organization and function.
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