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  • 1
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    The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-08-27
    Description: 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.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2946842/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2946842/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sekulic, Nikolina -- Bassett, Emily A -- Rogers, Danielle J -- Black, Ben E -- GM08275/GM/NIGMS NIH HHS/ -- GM82989/GM/NIGMS NIH HHS/ -- R01 GM082989/GM/NIGMS NIH HHS/ -- R01 GM082989-01A1/GM/NIGMS NIH HHS/ -- R01 GM082989-02/GM/NIGMS NIH HHS/ -- R01 GM082989-03/GM/NIGMS NIH HHS/ -- T32 GM008275/GM/NIGMS NIH HHS/ -- England -- Nature. 2010 Sep 16;467(7313):347-51. doi: 10.1038/nature09323. Epub 2010 Aug 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of Pennsylvania, School of Medicine, Philadelphia, Pennsylvania 19104-6059, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20739937" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Autoantigens/*chemistry/*metabolism ; Binding Sites ; Centromere/*chemistry/*metabolism ; Chromatin Assembly and Disassembly ; Chromosomal Proteins, Non-Histone/*chemistry/*metabolism ; Crystallography, X-Ray ; DNA/chemistry/metabolism ; Deuterium Exchange Measurement ; Epistasis, Genetic ; Histones/*chemistry/*metabolism ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Nucleosomes/chemistry/metabolism ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Rotation ; Scattering, Small Angle ; Structure-Activity Relationship ; Substrate Specificity
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Chromosomes. CENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2015-05-09
    Description: Inheritance of each chromosome depends upon its centromere. A histone H3 variant, centromere protein A (CENP-A), is essential for epigenetically marking centromere location. We find that CENP-A is quantitatively retained at the centromere upon which it is initially assembled. CENP-C binds to CENP-A nucleosomes and is a prime candidate to stabilize centromeric chromatin. Using purified components, we find that CENP-C reshapes the octameric histone core of CENP-A nucleosomes, rigidifies both surface and internal nucleosome structure, and modulates terminal DNA to match the loose wrap that is found on native CENP-A nucleosomes at functional human centromeres. Thus, CENP-C affects nucleosome shape and dynamics in a manner analogous to allosteric regulation of enzymes. CENP-C depletion leads to rapid removal of CENP-A from centromeres, indicating their collaboration in maintaining centromere identity.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4610723/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4610723/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Falk, Samantha J -- Guo, Lucie Y -- Sekulic, Nikolina -- Smoak, Evan M -- Mani, Tomoyasu -- Logsdon, Glennis A -- Gupta, Kushol -- Jansen, Lars E T -- Van Duyne, Gregory D -- Vinogradov, Sergei A -- Lampson, Michael A -- Black, Ben E -- CA186430/CA/NCI NIH HHS/ -- GM007229/GM/NIGMS NIH HHS/ -- GM008216/GM/NIGMS NIH HHS/ -- GM008275/GM/NIGMS NIH HHS/ -- GM082989/GM/NIGMS NIH HHS/ -- R01 GM082989/GM/NIGMS NIH HHS/ -- T32 GM008216/GM/NIGMS NIH HHS/ -- T32 GM008275/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2015 May 8;348(6235):699-703. doi: 10.1126/science.1259308.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. Graduate Program in Cell and Molecular Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. ; Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. Graduate Program in Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. ; Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. ; Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. Graduate Program in Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. Department of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA. ; Instituto Gulbenkian de Ciencia, 2780-156 Oeiras, Portugal. ; Graduate Program in Cell and Molecular Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. Graduate Program in Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. Department of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA. ; Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. Graduate Program in Cell and Molecular Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. Graduate Program in Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. blackbe@mail.med.upenn.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25954010" target="_blank"〉PubMed〈/a〉
    Keywords: Autoantigens/chemistry/genetics/*metabolism ; Centromere/chemistry/*metabolism/ultrastructure ; Chromosomal Proteins, Non-Histone/chemistry/genetics/*metabolism ; DNA/chemistry/metabolism ; Epigenesis, Genetic ; Fluorescence Resonance Energy Transfer ; Gene Knockdown Techniques ; Humans ; Nucleosomes/chemistry/*metabolism/ultrastructure ; Protein Structure, Secondary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
    Electronic Resource
    Electronic Resource
    Biometric analysis of Syngnathus abastev populations (2002)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of fish biology 60 (2002), S. 0 
    Details
    ISSN: 1095-8649
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Significant differences (ANOVA) in three out of six meristic characters and in 16 out of 18 morphometric characters were found among Syngnathus abaster caught in the River Danube at sites 900 km upwards from the mouth of the Black Sea, the fresh waters of Ukraine, the Black Sea and the Azov Sea. The Danube populations showed significantly greater values for antedorsal (aD) and anteanal (aA) distances, but considerably smaller values for postdorsal (pD) distance and head length (LH) than other populations analysed (Tukey-Kramer's test). The relation of total length (LT) to standard length (Ls) for the Danube populations was Ls= 0–97. Lt, the length-mass relationship was M=4.122. LT3.63 and the mean ± S.D. of Fulton condition factor was 0.34 ± 0.08.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1095-8649.2002.tb02448.x
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  • 4
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    Crystal structures of two domains of bifunctional enzyme: human PAPS synthetase (2005)
    International Union of Crystallography
    Details
    Publication Date: 2005-08-23
    Print ISSN: 0108-7673
    Electronic ISSN: 2053-2733
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Published by International Union of Crystallography
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