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Publication Abstract from PubMed

Survivin, a subunit of the Chromosome Passenger Complex, binds the N-terminal tail of histone H3, which is phosphorylated on T3 by Haspin kinase, and localizes the complex to the inner centromeres. We used X-ray crystallography to determine the residues of Survivin that are important in binding phosphomodified histone H3. Mutation of amino acids that interact with the histone N-terminus lowered in vitro tail binding affinity and reduced CPC recruitment to the inner centromere in cells, validating our solved structures. Phylogenetic analysis shows that non-mammalian vertebrates have two Survivin paralogs, which we name Class A and B. A distinguishing feature of these paralogs is H to R change in an amino acid that interacts with the histone T3 phosphate. The binding to histone tails of the human Class A paralog, which has a histidine at this position, is sensitive to changes around physiological pH, while Xenopus Survivin Class B is less so. Our data demonstrate that Survivin paralogs have different characteristics of phosphospecific binding to threonine-3 of histone H3, providing new insight into the biology of the inner centromere.

Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogs at inner centromeres.,Niedzialkowska E, Wang F, Porebski PJ, Minor W, Higgins JM, Stukenberg PT Mol Biol Cell. 2012 Feb 22. PMID:22357620^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.