Identification of a subdomain of CENP-B that is necessary and sufficient for localization to the human centromere

doi:10.1083/jcb.116.5.1081

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Identification of a subdomain of CENP-B that is necessary and sufficient for localization to the human centromere

AF Pluta, N Saitoh, I Goldberg and WC Earnshaw
Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.

We have combined in vivo and in vitro approaches to investigate the function of CENP-B, a major protein of human centromeric heterochromatin. Expression of epitope-tagged deletion derivatives of CENP-B in HeLa cells revealed that a single domain less than 158 residues from the amino terminus of the protein is sufficient to localize CENP-B to centromeres. Centromere localization was abolished if as few as 28 amino acids were removed from the amino terminus of CENP-B. The centromere localization signal of CENP-B can function in an autonomous fashion, relocating a fused bacterial enzyme to centromeres. The centromere localization domain of CENP-B specifically binds in vitro to a subset of alpha-satellite DNA monomers. These results suggest that the primary mechanism for localization of CENP-B to centromeres involves the recognition of a DNA sequence found at centromeres. Analysis of the distribution of this sequence in alpha- satellite DNA suggests that CENP-B binding may have profound effects on chromatin structure at centromeres.
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