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 Vermaak, D.
Right arrow Articles by Henikoff, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vermaak, D.
Right arrow Articles by Henikoff, S.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, November 2002, p. 7553-7561, Vol. 22, No. 21
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.21.7553-7561.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Centromere Targeting Element within the Histone Fold Domain of Cid

Danielle Vermaak,1 Hillary S. Hayden,1,{dagger} and Steven Henikoff1,2*

Howard Hughes Medical Institute,2 Basic Sciences Division, Fred Hutchinson Cancer Research Center, Seattle, Washington 981091

Received 29 May 2002/ Returned for modification 18 July 2002/ Accepted 30 July 2002

Centromeres require specialized nucleosomes; however, the mechanism of localization is unknown. Drosophila sp. centromeric nucleosomes contain the Cid H3-like protein. We have devised a strategy for identifying elements within Cid responsible for its localization to centromeres. By expressing Cid from divergent Drosophila species fused to green fluorescent protein in Drosophila melanogaster cells, we found that D. bipectinata Cid fails to localize to centromeres. Cid chimeras consisting of the D. bipectinata histone fold domain (HFD) replaced with segments from D. melanogaster identified loop I of the HFD as being critical for targeting to centromeres. Conversely, substitution of D. bipectinata loop I into D. melanogaster abolished centromeric targeting. In either case, loop I was the only segment capable of conferring targeting. Within loop I, we identified residues that are critical for targeting. Most mutations of conserved residues abolished targeting, and length reductions were deleterious. Taken together with the fact that H3 loop I makes numerous contacts with DNA and with the adaptive evolution of Cid, our results point to the importance of DNA specificity for targeting. We suggest that the process of deposition of (Cid.H4)2 tetramers allows for discriminating contacts to be made between loop I and DNA, providing the specificity needed for targeting.


* Corresponding author. Mailing address: Fred Hutchinson Cancer Research Center, 1100 Fairview Ave. N., Seattle, WA 98109. Phone: (206) 667-4515. Fax: (206) 667-5889. E-mail: steveh{at}fhcrc.org.

{dagger} Present address: LifeSpan BioSciences, Inc., Seattle, WA 98121.


Molecular and Cellular Biology, November 2002, p. 7553-7561, Vol. 22, No. 21
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.21.7553-7561.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Hirsch, C. D., Wu, Y., Yan, H., Jiang, J. (2009). Lineage-Specific Adaptive Evolution of the Centromeric Protein CENH3 in Diploid and Allotetraploid Oryza Species. Mol Biol Evol 26: 2877-2885 [Abstract] [Full Text]  
  • Vermaak, D., Bayes, J. J., Malik, H. S. (2009). A Surrogate Approach to Study the Evolution of Noncoding DNA Elements That Organize Eukaryotic Genomes. J Hered 100: 624-636 [Abstract] [Full Text]  
  • Dalal, Y., Furuyama, T., Vermaak, D., Henikoff, S. (2007). Inaugural Article: Structure, dynamics, and evolution of centromeric nucleosomes. Proc. Natl. Acad. Sci. USA 104: 15974-15981 [Abstract] [Full Text]  
  • Furuyama, S., Biggins, S. (2007). Centromere identity is specified by a single centromeric nucleosome in budding yeast. Proc. Natl. Acad. Sci. USA 104: 14706-14711 [Abstract] [Full Text]  
  • Moreno-Moreno, O., Torras-Llort, M., Azorin, F. (2006). Proteolysis restricts localization of CID, the centromere-specific histone H3 variant of Drosophila, to centromeres. Nucleic Acids Res 34: 6247-6255 [Abstract] [Full Text]  
  • Baker, R. E., Rogers, K. (2006). Phylogenetic Analysis of Fungal Centromere H3 Proteins. Genetics 174: 1481-1492 [Abstract] [Full Text]  
  • Lermontova, I., Schubert, V., Fuchs, J., Klatte, S., Macas, J., Schubert, I. (2006). Loading of Arabidopsis Centromeric Histone CENH3 Occurs Mainly during G2 and Requires the Presence of the Histone Fold Domain. Plant Cell 18: 2443-2451 [Abstract] [Full Text]  
  • Nagaki, K., Kashihara, K., Murata, M. (2005). Visualization of Diffuse Centromeres with Centromere-Specific Histone H3 in the Holocentric Plant Luzula nivea. Plant Cell 17: 1886-1893 [Abstract] [Full Text]  
  • Kamakaka, R. T., Biggins, S. (2005). Histone variants: deviants?. Genes Dev. 19: 295-316 [Abstract] [Full Text]  
  • Morey, L., Barnes, K., Chen, Y., Fitzgerald-Hayes, M., Baker, R. E. (2004). The Histone Fold Domain of Cse4 Is Sufficient for CEN Targeting and Propagation of Active Centromeres in Budding Yeast. Eukaryot Cell 3: 1533-1543 [Abstract] [Full Text]  
  • Cooper, J. L., Henikoff, S. (2004). Adaptive Evolution of the Histone Fold Domain in Centromeric Histones. Mol Biol Evol 21: 1712-1718 [Abstract] [Full Text]