At the right place at the right time: novel CENP-A binding proteins shed light on centromere assembly

Centromeres, the chromosomal loci that form the sites of attachment for spindle microtubules during mitosis, are identified by a unique chromatin structure generated by nucleosomes containing the histone H3 variant CENP-A. The apparent epigenetic mode of centromere inheritance across mitotic and mei...

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Bibliographic Details
Published in:Chromosoma 2009-10, Vol.118 (5), p.567-574
Main Authors: Silva, Mariana C. C, Jansen, Lars E. T
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing - physiology
Animal Genetics and Genomics
Animals
Autoantigens - metabolism
Biochemistry
Biomedical and Life Sciences
Carrier Proteins - physiology
Cell Biology
Cell Cycle - physiology
Centromere - physiology
Centromere Protein A
Chromatin - physiology
Chromosomal Proteins, Non-Histone - metabolism
Developmental Biology
Eukaryotic Microbiology
Human Genetics
Humans
Life Sciences
Mini-Review
Schizosaccharomyces pombe
Schizosaccharomyces pombe Proteins - physiology
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Summary:Centromeres, the chromosomal loci that form the sites of attachment for spindle microtubules during mitosis, are identified by a unique chromatin structure generated by nucleosomes containing the histone H3 variant CENP-A. The apparent epigenetic mode of centromere inheritance across mitotic and meiotic divisions has generated much interest in how CENP-A assembly occurs and how structurally divergent centromeric nucleosomes can specify the centromere complex. Although a substantial number of proteins have been implicated in centromere assembly, factors that can bind CENP-A specifically and deliver nascent protein to the centromere were, thus far, lacking. Several recent reports on experiments in fission yeast and human cells have now shown significant progress on this problem. Here, we discuss these new developments and their implications for epigenetic centromere inheritance.
ISSN:0009-5915
1432-0886
DOI:10.1007/s00412-009-0227-3