Histone post-translational modifications

Histone post-translational modifications are covalent modifications of histones by phosphorylation on serine or threonine residues, methylation on lysine or arginine, acetylation and deacetylation of lysines, ubiquitylation of lysines and sumoylation of lysines. Histone modifications are proposed to affect chromosome structure and function, for instance during transcription and chromatin remodelling processes.

Latest Research and Reviews

  • Research | | open

    Kinetochore function depends on H4K20 monomethylation in centromeric nucleosomes but the underlying mechanism is unclear. Here, the authors provide evidence that the centromere-specific nucleosome subunit CENP-A facilitates H4K20 methylation by enabling a conformational change of the H4 N-terminal tail.

    • Yasuhiro Arimura
    • , Hiroaki Tachiwana
    • , Hiroki Takagi
    • , Tetsuya Hori
    • , Hiroshi Kimura
    • , Tatsuo Fukagawa
    •  & Hitoshi Kurumizaka
  • Research | | open

    In Drosophila, the Calypso–ASX complex catalyzes H2A deubiquitination and aids Polycomb in transcriptional silencing. Here the authors show that the orthologous complex, BAP1.com, promotes gene activation by counteracting PRC1-mediated gene silencing.

    • Antoine Campagne
    • , Ming-Kang Lee
    • , Dina Zielinski
    • , Audrey Michaud
    • , Stéphanie Le Corre
    • , Florent Dingli
    • , Hong Chen
    • , Lara Z. Shahidian
    • , Ivaylo Vassilev
    • , Nicolas Servant
    • , Damarys Loew
    • , Eric Pasmant
    • , Sophie Postel-Vinay
    • , Michel Wassef
    •  & Raphaël Margueron
  • Research | | open

    Akiko Okita et al. demonstrate that heterochromatin suppresses gross chromosomal rearrangements by repressing Tfs1/TFIIS-dependent transcription of repetitive sequences. This study underscores the role of heterochromatin for maintaining chromosome stability.

    • Akiko K. Okita
    • , Faria Zafar
    • , Jie Su
    • , Dayalini Weerasekara
    • , Takuya Kajitani
    • , Tatsuro S. Takahashi
    • , Hiroshi Kimura
    • , Yota Murakami
    • , Hisao Masukata
    •  & Takuro Nakagawa
  • Research | | open

    Phosphorylation of CENP-A on serine 7 has been proposed to control centromere assembly and function. Here, the authors use gene targeting at both endogenous CENP-A alleles and gene replacement in human cells to demonstrate that CENP-A that cannot be phosphorylated at serine 7 maintains correct CENP-C recruitment, faithful chromosome segregation and long-term cell viability.

    • Viviana Barra
    • , Glennis A. Logsdon
    • , Andrea Scelfo
    • , Sebastian Hoffmann
    • , Solène Hervé
    • , Aaron Aslanian
    • , Yael Nechemia-Arbely
    • , Don W. Cleveland
    • , Ben E. Black
    •  & Daniele Fachinetti
  • Research | | open

    The demethylase activity of KDM5A is allosterically enhanced by binding of histone H3 to its PHD1 reader domain, through an unknown mechanism. Here the authors show that the PHD1 domain drives ligand-induced allosteric stimulation by stabilizing the binding of substrate to the catalytic domain.

    • James E. Longbotham
    • , Cynthia M. Chio
    • , Venkatasubramanian Dharmarajan
    • , Michael J. Trnka
    • , Idelisse Ortiz Torres
    • , Devrishi Goswami
    • , Karen Ruiz
    • , Alma L. Burlingame
    • , Patrick R. Griffin
    •  & Danica Galonić Fujimori
  • Research | | open

    MLL3 and MLL4 are members of the SET1/MLL family of histone H3K4 methyltransferases, which are responsible for monomethylating histone H3K4 on enhancers. Here the authors show that an extended PHD domain (ePHD6) in MLL3 and MLL4 specifically recognizes an H4H18-containing fragment of histone H4, and that modifications of residues surrounding H4H18 modulate H4 binding to MLL3/4.

    • Yanli Liu
    • , Su Qin
    • , Tsai-Yu Chen
    • , Ming Lei
    • , Shilpa S. Dhar
    • , Jolene Caifeng Ho
    • , Aiping Dong
    • , Peter Loppnau
    • , Yanjun Li
    • , Min Gyu Lee
    •  & Jinrong Min

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