This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cortés, A.
Right arrow Articles by Azorín, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cortés, A.
Right arrow Articles by Azorín, F.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, June 2000, p. 3860-3869, Vol. 20, No. 11
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

DDP1, a Heterochromatin-Associated Multi-KH-Domain Protein of Drosophila melanogaster, Interacts Specifically with Centromeric Satellite DNA Sequences

Alfred Cortés and Fernando Azorín*

Departament de Biologia Molecular i Cellular, Institut de Biologia Molecular de Barcelona, CSIC, 08034 Barcelona, Spain

Received 8 December 1999/Returned for modification 21 January 2000/Accepted 2 March 2000

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.

* Corresponding author. Mailing address: Departament de Biologia Molecular i Cellular, Institut de Biologia Molecular de Barcelona, CID-CSIC, Jordi Girona Salgado 18-26, 08034 Barcelona, Spain. Phone: 3493-4006137. Fax: 3493-2045904. E-mail: fambmc{at}cid.csic.es.

Molecular and Cellular Biology, June 2000, p. 3860-3869, Vol. 20, No. 11
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Zhou, J., Wang, Q., Chen, L.-L., Carmichael, G. G. (2008). On the mechanism of induction of heterochromatin by the RNA-binding protein vigilin. RNA 14: 1773-1781 [Abstract] [Full Text]  
  • Brykailo, M. A., Corbett, A. H., Fridovich-Keil, J. L. (2007). Functional overlap between conserved and diverged KH domains in Saccharomyces cerevisiae SCP160. Nucleic Acids Res 35: 1108-1118 [Abstract] [Full Text]  
  • Musunuru, K., Darnell, R. B. (2004). Determination and augmentation of RNA sequence specificity of the Nova K-homology domains. Nucleic Acids Res 32: 4852-4861 [Abstract] [Full Text]  
  • Li, A.-m., Vargas, C. A., Brykailo, M. A., Openo, K. K., Corbett, A. H., Fridovich-Keil, J. L. (2004). Both KH and non-KH domain sequences are required for polyribosome association of Scp160p in yeast. Nucleic Acids Res 32: 4768-4775 [Abstract] [Full Text]  
  • Mendelsohn, B. A., Li, A.-m., Vargas, C. A., Riehman, K., Watson, A., Fridovich-Keil, J. L. (2003). Genetic and biochemical interactions between SCP160 and EAP1 in yeast. Nucleic Acids Res 31: 5838-5847 [Abstract] [Full Text]  
  • Goolsby, K. M., Shapiro, D. J. (2003). 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 Res 31: 5644-5653 [Abstract] [Full Text]  
  • Li, A.-M., Watson, A., Fridovich-Keil, J. L. (2003). Scp160p associates with specific mRNAs in yeast. Nucleic Acids Res 31: 1830-1837 [Abstract] [Full Text]  
  • Smith, R. K., Carroll, P. M., Allard, J. D., Simon, M. A. (2002). MASK, a large ankyrin repeat and KH domain-containing protein involved in Drosophila receptor tyrosine kinase signaling. Development 129: 71-82 [Abstract] [Full Text]  
  • Frey, S., Pool, M., Seedorf, M. (2001). Scp160p, an RNA-binding, Polysome-associated Protein, Localizes to the Endoplasmic Reticulum of Saccharomyces cerevisiae in a Microtubule-dependent Manner. J. Biol. Chem. 276: 15905-15912 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»