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  1. Article ; Online: The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres.

    Sekulic, Nikolina / Bassett, Emily A / Rogers, Danielle J / Black, Ben E

    Nature

    2010  Volume 467, Issue 7313, Page(s) 347–351

    Abstract: Centromeres are specified epigenetically, and the histone H3 variant CENP-A is assembled into the chromatin of all active centromeres. Divergence from H3 raises the possibility that CENP-A generates unique chromatin features to mark physically centromere ...

    Abstract Centromeres are specified epigenetically, and the histone H3 variant CENP-A is assembled into the chromatin of all active centromeres. Divergence from H3 raises the possibility that CENP-A generates unique chromatin features to mark physically centromere location. Here we report the crystal structure of a subnucleosomal heterotetramer, human (CENP-A-H4)(2), that reveals three distinguishing properties encoded by the residues that comprise the CENP-A targeting domain (CATD; ref. 2): (1) a CENP-A-CENP-A interface that is substantially rotated relative to the H3-H3 interface; (2) a protruding loop L1 of the opposite charge as that on H3; and (3) strong hydrophobic contacts that rigidify the CENP-A-H4 interface. Residues involved in the CENP-A-CENP-A rotation are required for efficient incorporation into centromeric chromatin, indicating specificity for an unconventional nucleosome shape. DNA topological analysis indicates that CENP-A-containing nucleosomes are octameric with conventional left-handed DNA wrapping, in contrast to other recent proposals. Our results indicate that CENP-A marks centromere location by restructuring the nucleosome from within its folded histone core.
    MeSH term(s) Amino Acid Sequence ; Autoantigens/chemistry ; Autoantigens/metabolism ; Binding Sites ; Centromere/chemistry ; Centromere/metabolism ; Centromere Protein A ; Chromatin Assembly and Disassembly ; Chromosomal Proteins, Non-Histone/chemistry ; Chromosomal Proteins, Non-Histone/metabolism ; Crystallography, X-Ray ; DNA/chemistry ; DNA/metabolism ; Deuterium Exchange Measurement ; Epistasis, Genetic ; Histones/chemistry ; Histones/metabolism ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Nucleosomes/chemistry ; Nucleosomes/metabolism ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Rotation ; Scattering, Small Angle ; Structure-Activity Relationship ; Substrate Specificity
    Chemical Substances Autoantigens ; CENPA protein, human ; Centromere Protein A ; Chromosomal Proteins, Non-Histone ; Histones ; Nucleosomes ; DNA (9007-49-2)
    Language English
    Publishing date 2010-08-25
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/nature09323
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: HJURP Uses Distinct CENP-A Surfaces to Recognize and to Stabilize CENP-A/Histone H4 for Centromere Assembly

    Bassett, Emily A / DeNizio, Jamie / Barnhart-Dailey, Meghan C / Panchenko, Tanya / Sekulic, Nikolina / Rogers, Danielle J / Foltz, Daniel R / Black, Ben E

    Developmental cell. 2012 Apr. 17, v. 22, no. 4

    2012  

    Abstract: Centromeres are defined by the presence of chromatin containing the histone H3 variant, CENP-A, whose assembly into nucleosomes requires the chromatin assembly factor HJURP. We find that whereas surface-exposed residues in the CENP-A targeting domain ( ... ...

    Abstract Centromeres are defined by the presence of chromatin containing the histone H3 variant, CENP-A, whose assembly into nucleosomes requires the chromatin assembly factor HJURP. We find that whereas surface-exposed residues in the CENP-A targeting domain (CATD) are the primary sequence determinants for HJURP recognition, buried CATD residues that generate rigidity with H4 are also required for efficient incorporation into centromeres. HJURP contact points adjacent to the CATD on the CENP-A surface are not used for binding specificity but rather to transmit stability broadly throughout the histone fold domains of both CENP-A and H4. Furthermore, an intact CENP-A/CENP-A interface is a requirement for stable chromatin incorporation immediately upon HJURP-mediated assembly. These data offer insight into the mechanism by which HJURP discriminates CENP-A from bulk histone complexes and chaperones CENP-A/H4 for a substantial portion of the cell cycle prior to mediating chromatin assembly at the centromere.
    Keywords cell cycle ; centromeres ; histones ; nucleosomes
    Language English
    Dates of publication 2012-0417
    Size p. 749-762.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2012.02.001
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: DNA binding restricts the intrinsic conformational flexibility of methyl CpG binding protein 2 (MeCP2).

    Hansen, Jeffrey C / Wexler, Brian B / Rogers, Danielle J / Hite, Kristopher C / Panchenko, Tanya / Ajith, Sandya / Black, Ben E

    The Journal of biological chemistry

    2011  Volume 286, Issue 21, Page(s) 18938–18948

    Abstract: Mass spectrometry-based hydrogen/deuterium exchange (H/DX) has been used to define the polypeptide backbone dynamics of full-length methyl CpG binding protein 2 (MeCP2) when free in solution and when bound to unmethylated and methylated DNA. Essentially ... ...

    Abstract Mass spectrometry-based hydrogen/deuterium exchange (H/DX) has been used to define the polypeptide backbone dynamics of full-length methyl CpG binding protein 2 (MeCP2) when free in solution and when bound to unmethylated and methylated DNA. Essentially the entire MeCP2 polypeptide chain underwent H/DX at rates faster than could be measured (i.e. complete exchange in ≤10 s), with the exception of the methyl DNA binding domain (MBD). Even the H/DX of the MBD was rapid compared with that of a typical globular protein. Thus, there is no single tertiary structure of MeCP2. Rather, the full-length protein rapidly samples many different conformations when free in solution. When MeCP2 binds to unmethylated DNA, H/DX is slowed several orders of magnitude throughout the MBD. Binding of MeCP2 to methylated DNA led to additional minor H/DX protection, and only locally within the N-terminal portion of the MBD. H/DX also was used to examine the structural dynamics of the isolated MBD carrying three frequent mutations associated with Rett syndrome. The effects of the mutations ranged from very little (R106W) to a substantial increase in conformational sampling (F155S). Our H/DX results have yielded fine resolution mapping of the structure of full-length MeCP2 in the absence and presence of DNA, provided a biochemical basis for understanding MeCP2 function in normal cells, and predicted potential approaches for the treatment of a subset of RTT cases caused by point mutations that destabilize the MBD.
    MeSH term(s) Amino Acid Substitution ; DNA/chemistry ; DNA/genetics ; DNA/metabolism ; DNA Methylation ; Humans ; Methyl-CpG-Binding Protein 2/chemistry ; Methyl-CpG-Binding Protein 2/genetics ; Methyl-CpG-Binding Protein 2/metabolism ; Mutation, Missense ; Peptide Mapping ; Protein Binding ; Protein Conformation ; Protein Stability ; Rett Syndrome/genetics ; Rett Syndrome/metabolism
    Chemical Substances MECP2 protein, human ; Methyl-CpG-Binding Protein 2 ; DNA (9007-49-2)
    Language English
    Publishing date 2011-04-04
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M111.234609
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: HJURP uses distinct CENP-A surfaces to recognize and to stabilize CENP-A/histone H4 for centromere assembly.

    Bassett, Emily A / DeNizio, Jamie / Barnhart-Dailey, Meghan C / Panchenko, Tanya / Sekulic, Nikolina / Rogers, Danielle J / Foltz, Daniel R / Black, Ben E

    Developmental cell

    2012  Volume 22, Issue 4, Page(s) 749–762

    Abstract: Centromeres are defined by the presence of chromatin containing the histone H3 variant, CENP-A, whose assembly into nucleosomes requires the chromatin assembly factor HJURP. We find that whereas surface-exposed residues in the CENP-A targeting domain ( ... ...

    Abstract Centromeres are defined by the presence of chromatin containing the histone H3 variant, CENP-A, whose assembly into nucleosomes requires the chromatin assembly factor HJURP. We find that whereas surface-exposed residues in the CENP-A targeting domain (CATD) are the primary sequence determinants for HJURP recognition, buried CATD residues that generate rigidity with H4 are also required for efficient incorporation into centromeres. HJURP contact points adjacent to the CATD on the CENP-A surface are not used for binding specificity but rather to transmit stability broadly throughout the histone fold domains of both CENP-A and H4. Furthermore, an intact CENP-A/CENP-A interface is a requirement for stable chromatin incorporation immediately upon HJURP-mediated assembly. These data offer insight into the mechanism by which HJURP discriminates CENP-A from bulk histone complexes and chaperones CENP-A/H4 for a substantial portion of the cell cycle prior to mediating chromatin assembly at the centromere.
    MeSH term(s) Amino Acid Sequence ; Autoantigens/chemistry ; Autoantigens/metabolism ; Binding Sites ; Cell Cycle ; Centromere/physiology ; Centromere Protein A ; Chromatin Assembly and Disassembly ; Chromosomal Proteins, Non-Histone/chemistry ; Chromosomal Proteins, Non-Histone/metabolism ; DNA-Binding Proteins/metabolism ; HeLa Cells ; Histones/chemistry ; Histones/metabolism ; Humans ; Immunoblotting ; Mass Spectrometry ; Molecular Sequence Data ; Nucleosomes/physiology ; Protein Binding ; Protein Conformation ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Homology, Amino Acid
    Chemical Substances Autoantigens ; CENPA protein, human ; Centromere Protein A ; Chromosomal Proteins, Non-Histone ; DNA-Binding Proteins ; HJURP protein, human ; Histones ; Nucleosomes ; Recombinant Proteins
    Language English
    Publishing date 2012-03-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2012.02.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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