Histone Ubiquitination: Triggering Gene Activity

Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, USA.
Molecular cell (Impact Factor: 14.46). 04/2008; 29(6):653-63. DOI: 10.1016/j.molcel.2008.02.014
Source: PubMed

ABSTRACT Recently, many of the enzymes responsible for the addition and removal of ubiquitin from the histones H2A and H2B have been identified and characterized. From these studies, it has become clear that H2A and H2B ubiquitination play critical roles in regulating many processes within the nucleus, including transcription initiation and elongation, silencing, and DNA repair. In this review, we present the enzymes involved in H2A and H2B ubiquitination and discuss new evidence that links histone ubiquitination to other chromatin modifications, which has provided a model for the role of H2B ubiquitination, in particular, in transcription initiation and elongation.

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Available from: Jerry L Workman, Jul 24, 2015
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    • "Please cite this article in press as: Gatti et al., RNF168 Promotes Noncanonical K27 Ubiquitination to Signal DNA Damage, Cell Reports (2015), http:// the inhibitory effect of different deubiquitinating enzymes. Specifically , USP3 and USP16 counteract H2A ubiquitination (Weake and Workman, 2008), BRCC36 displays selectivity for K6 and K63 modulating the signals generated by apical ubiquitin ligases (Sobhian et al., 2007), and OTUB1 suppresses RNF168- mediated ubiquitination independently of its catalytic activity, by inhibiting UBC13 (Nakada et al., 2010). An additional case of negative regulation of DDR signaling is provided by the two HECT-type ubiquitin ligases TRIP12 and UBR5, which control the accumulation of RNF168 to DDR foci, thereby preventing excessive histone ubiquitination (Gudjonsson et al., 2012). "
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    ABSTRACT: Graphical Abstract Highlights d RNF168 mediates K27 ubiquitination of histone H2As d K27 ubiquitination is the major ubiquitin mark on chromatin upon DNA damage d K27 is strictly required for proper activation of the DNA damage response d 53BP1, Rap80, RNF168, and RNF169 directly recognize the K27 linkage Authors In Brief Gatti et al. demonstrate that cells respond to genotoxic stress by inducing K27 ubiquitination, a modification essential for activation of the DNA damage response and DNA repair. K27 ubiquitination is generated by RNF168 and targets the N-terminal tail of histone H2As.
    Cell Reports 01/2015; 10(13):1-13. DOI:10.1016/j.celrep.2014.12.021 · 7.21 Impact Factor
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    • "Shown is one biological repeat with three technical repeats. HUB1 encodes an E3 ubiquitin ligase that monoubiquitinates H2B, and the enrichment of H2Bub1 is usually associated with gene activation (Sun and Allis, 2002; Weake and Workman, 2008; Bourbousse et al., 2012). HUB1-mediated H2Bub1 is required for the activation of FLC and its homologs to control flowering time (Cao et al., 2008). "
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    ABSTRACT: Disease resistance (R) genes are key components in plant immunity. Here we show that Arabidopsis E3 ubiquitin ligase genes HUB1 (HISTONE MONOUBIQUITINATION1) and HUB2 regulate the expression of the R genes SNC1 (SUPPRESSOR OF npr1-1, CONSTITUTIVE1)and RPP4 (RESISTANCE TO PERONOSPORA PARASITICA 4). An increase of SNC1 expression induces constitutive immune responses in the bon1 (bonzai1) mutant, and the loss of HUB1 or HUB2 function reduces SNC1 upregulation and suppresses the bon1 autoimmune phenotypes. HUB1 and HUB2 mediate H2B monoubiquitination directly at the SNC1 R gene locus to regulate its expression. In addition, SNC1 and HUB1 transcripts are moderately up-regulated by pathogen infection and H2B monoubiquitination at SNC1 is enhanced by pathogen infection. Together, this study indicates that H2B monoubiquitination at the R gene locus regulates its expression and this histone modification at the R gene locus has an impact on immune responses in plants.
    Plant physiology 03/2014; 165(1). DOI:10.1104/pp.113.227801 · 7.39 Impact Factor
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    • "This histone modification can be removed by deubiquitinating enzymes (DUBs), which are also known as ubiquitin proteases (UBPs) (Zhang, 2003). Histone H2B monoubiquitination (H2Bub) is part of a general mechanism that influences transcriptional activity positively (Weake and Workman, 2008). H2Bub was found to facilitate RNA Pol II processivity by favouring DNA accessibility, by helping to recruit the histone chaperone Facilitates Chromatin Transcription (FACT) and/or ensuring nucleosome reassembly upon RNA Pol II elongation (Belotserkovskaya et al., 2003; Pavri et al., 2006; Fleming et al., 2008; Xin et al., 2009; Fierz et al., 2011). "
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    ABSTRACT: Research on the functional properties of nucleosome structure and composition dynamics has revealed that chromatin-level regulation is an essential component of light signalling and clock function in plants, two processes that rely extensively on transcriptional controls. In particular, several types of histone post-translational modifications and chromatin-bound factors act sequentially or in combination to establish transcriptional patterns and to fine-tune the transcript abundance of a large repertoire of light-responsive genes and clock components. Cytogenetic approaches have also identified light-induced higher-order chromatin changes that dynamically organize the condensation of chromosomal domains into sub-nuclear foci containing silenced repeat elements. In this review, we report recently identified molecular actors that establish chromatin state dynamics in response to light signals such as photoperiod, intensity, and spectral quality. We also highlight the chromatin-dependent mechanisms that contribute to the 24-h circadian gene expression and its impact on plant physiology and development. The commonalities and contrasts of light- and clock-associated chromatin-based mechanisms are discussed, with particular emphasis on their impact on the selective regulation and rapid modulation of responsive genes.
    Journal of Experimental Botany 02/2014; DOI:10.1093/jxb/eru011 · 5.79 Impact Factor
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