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XB-ART-44894
Mol Biol Cell April 1, 2012; 23 (8): 1457-66.

Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres.

Niedzialkowska E , Wang F , Porebski PJ , Minor W , Higgins JM , Stukenberg PT .


Abstract
Survivin, a subunit of the chromosome passenger complex (CPC), 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 nonmammalian vertebrates have two Survivin paralogues, which we name class A and B. A distinguishing feature of these paralogues is an 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 paralogue, which has a histidine at this position, is sensitive to changes around physiological pH, whereas Xenopus Survivin class B is less so. Our data demonstrate that Survivin paralogues have different characteristics of phosphospecific binding to threonine-3 of histone H3, providing new insight into the biology of the inner centromere.

PubMed ID: 22357620
PMC ID: PMC3327328
Article link: Mol Biol Cell
Grant support: GM053163 NIGMS NIH HHS , R01 GM053163-18 NIGMS NIH HHS , R01GM063045 NIGMS NIH HHS , R01GM074210 NIGMS NIH HHS , R01GM081576 NIGMS NIH HHS , R01 GM053163 NIGMS NIH HHS , R01 GM063045 NIGMS NIH HHS , R01 GM081576 NIGMS NIH HHS , R01 GM074210 NIGMS NIH HHS

Genes referenced: aurkb birc5.1 myc


Article Images: [+] show captions
References:
Adams, 2000, Pubmed, Xenbase [+]


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