Active genes are tri-methylated at K4 of histone H3

Santos‐Rosa, Helena; Schneider, Robert; Bannister, Andrew J.; Sherriff, Julia A; Bernstein, B; Emre, N. C. Tolga; Schreiber, Stuart L.; Mellor, Jane; Kouzarides, Tony

doi:10.1038/nature01080

Cited by 1,919 publications

(1,671 citation statements)

References 19 publications

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“…As di-and trimethylation at histone H3 lysine 4 are correlated with gene activation (Noma and Grewal, 2002;Santos-Rosa et al, 2002), we determined whether histone H3 was trimethylated at lysine 4 on the kB site of the MMP9 promoter on p52 or Hut-78 overexpression by chromatin immunoprecipitation (ChIP) assays. A robust histone H3K4 trimethylation was detected on the MMP9 but not on the IkBa promoter on p52 or Hut-78 overexpression in NIH3T3 cells (Figure 6b).…”

Section: Rhd Nls Grr Ankyrin P65mentioning

confidence: 99%

Matrix Metalloproteinase-9 gene induction by a truncated oncogenic NF-κB2 protein involves the recruitment of MLL1 and MLL2 H3K4 histone methyltransferase complexes

et al. 2009

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Constitutive nuclear factor (NF)-jB activation in haematological malignancies is caused in several cases by loss of function mutations within the coding sequence of NF-jB inhibitory molecules such as IjBa or p100. Hut-78, a truncated form of p100, constitutively generates p52 and contributes to the development of T-cell lymphomas but the molecular mechanism underlying this oncogenic potential remains unclear. We show here that MMP9 gene expression is induced through the alternative NF-jB-activating pathway in fibroblasts and also on Hut-78 or p52 overexpression in fibroblasts as well as in lymphoma cells. p52 is critical for Hut-78-mediated MMP9 gene induction as a Hut-78 mutant as well as other truncated NF-jB2 proteins that are not processed into p52 failed to induce the expression of this metalloproteinase. Conversely, MMP9 gene expression is impaired in p52-depleted HUT-78 cells. Interestingly, MLL1 and MLL2 H3K4 methyltransferase complexes are tethered by p52 on the MMP9 but not on the IjBa promoter, and the H3K4 trimethyltransferase activity recruited on the MMP9 promoter is impaired in p52-depleted HUT-78 cells. Moreover, MLL1 and MLL2 are associated with Hut-78 in a native chromatin-enriched extract. Thus, we identified a molecular mechanism by which the recruitment of a H3K4 histone methyltransferase complex on the promoter of a NF-jB-dependent gene induces its expression and potentially the invasive potential of lymphoma cells harbouring constitutive activity of the alternative NF-jB-activating pathway.

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Section: Rhd Nls Grr Ankyrin P65mentioning

confidence: 99%

Matrix Metalloproteinase-9 gene induction by a truncated oncogenic NF-κB2 protein involves the recruitment of MLL1 and MLL2 H3K4 histone methyltransferase complexes

et al. 2009

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“…The TRITHORAX (TRX) family of proteins, including Drosophila Trithorax (Trx), mammalian Mixed lineage leukemia protein 1‐4 (MLL1‐4) and ARABIDOPSIS HOMOLOG of TRITHORAX 1‐2 (ATX1‐2), form a phylogenetic subgroup distinct from yeast Set1. Yeast SET1 is the sole methyltransferase acting on lysine 4 of histone H3, and is responsible for the mono, di‐ and tri‐methylation of H3K4 (Bernstein et al ., 2002; Santos‐Rosa et al ., 2002). Arabidopsis ATX1 tri‐methylates H3K4 at specific genes involved in multiple biological processes, such as flowering time regulation, dehydration stress responses and flower organ development (Alvarez‐Venegas et al ., 2003; Saleh et al ., 2007; Pien et al ., 2008; Ding et al ., 2011a,b, 2012a,b).…”

Section: Introductionmentioning

confidence: 99%

SIP1 participates in regulation of flowering time in rice by recruiting OsTrx1 to Ehd1

et al. 2018

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Summary Flowering time (heading date) in rice (Oryza sativa) is an important agronomic trait that determines yield. The levels of histone H3 lysine 4 trimethylation (H3K4me3) modulated by TRITHORAX‐like proteins regulate gene transcription, flowering time and environmental stress responses. However, plant TRITHORAX‐like proteins have no known DNA‐binding domain, and therefore the mechanism that gives sequence specificity to these proteins remains unclear.Here, we show that the rice TRITHORAX‐like protein OsTrx1 is recruited to its target, Early heading date 1 (Ehd1), by the C2H2 zinc finger protein SDG723/OsTrx1/OsSET33 Interaction Protein 1 (SIP1). SIP1 binds to the promoter of Ehd1 and interacts with OsTrx1. Mutations in SIP1 led to a late heading date under long‐day and short‐day conditions. Defects in OsTrx1 or SIP1 led to reduced H3K4me3 levels at Ehd1, thus reducing Ehd1 expression.Together, our results show that the transcription factor SIP1 interacts with OxTrx1, allowing OsTrx1 to specifically target Ehd1, altering H3K4me3 levels, increasing Ehd1 expression and thereby promoting flowering.

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“…A further level of complexity occurs with lysine residues, which can be methylated or acetylated, and methylation exists as mono-, di-or tri-methylation, in which the type of methylation event has been linked to the functional consequence on gene activity (Kouzarides, 2007). For example, tri-methylation of K4 in histone H3 correlates with transcriptional activity (Santos-Rosa et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

Lysine methylation regulates the pRb tumour suppressor protein

et al. 2010

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The pRb tumour suppressor protein has a central role in coordinating early cell cycle progression. An important level of control imposed on pRb occurs through posttranslational modification, for example, phosphorylation. We describe here a new level of regulation on pRb, mediated through the targeted methylation of lysine residues, by the methyltransferase Set7/9. Set7/9 methylates the C-terminal region of pRb, both in vitro and in cells, and methylated pRb interacts with heterochromatin protein HP1. pRb methylation is required for pRbdependent cell cycle arrest and transcriptional repression, as well as pRb-dependent differentiation. Our results indicate that methylation can influence the properties of pRb, and raise the interesting possibility that methylation modulates pRb tumour suppressor activity.

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Active genes are tri-methylated at K4 of histone H3

Cited by 1,919 publications

References 19 publications

Matrix Metalloproteinase-9 gene induction by a truncated oncogenic NF-κB2 protein involves the recruitment of MLL1 and MLL2 H3K4 histone methyltransferase complexes

Matrix Metalloproteinase-9 gene induction by a truncated oncogenic NF-κB2 protein involves the recruitment of MLL1 and MLL2 H3K4 histone methyltransferase complexes

SIP1 participates in regulation of flowering time in rice by recruiting OsTrx1 to Ehd1

Lysine methylation regulates the pRb tumour suppressor protein

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