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Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres
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 bindin...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3327328/ https://www.ncbi.nlm.nih.gov/pubmed/22357620 http://dx.doi.org/10.1091/mbc.E11-11-0904 |
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author | Niedzialkowska, Ewa Wang, Fangwei Porebski, Przemyslaw J. Minor, Wladek Higgins, Jonathan M. G. Stukenberg, P. Todd |
author_facet | Niedzialkowska, Ewa Wang, Fangwei Porebski, Przemyslaw J. Minor, Wladek Higgins, Jonathan M. G. Stukenberg, P. Todd |
author_sort | Niedzialkowska, Ewa |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3327328 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-33273282012-06-30 Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres Niedzialkowska, Ewa Wang, Fangwei Porebski, Przemyslaw J. Minor, Wladek Higgins, Jonathan M. G. Stukenberg, P. Todd Mol Biol Cell Articles 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. The American Society for Cell Biology 2012-04-15 /pmc/articles/PMC3327328/ /pubmed/22357620 http://dx.doi.org/10.1091/mbc.E11-11-0904 Text en © 2012 Niedzialkowska et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Niedzialkowska, Ewa Wang, Fangwei Porebski, Przemyslaw J. Minor, Wladek Higgins, Jonathan M. G. Stukenberg, P. Todd Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres |
title | Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres |
title_full | Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres |
title_fullStr | Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres |
title_full_unstemmed | Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres |
title_short | Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres |
title_sort | molecular basis for phosphospecific recognition of histone h3 tails by survivin paralogues at inner centromeres |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3327328/ https://www.ncbi.nlm.nih.gov/pubmed/22357620 http://dx.doi.org/10.1091/mbc.E11-11-0904 |
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