The role of histone H2A and H2B post-translational modifications in transcription: A genomic perspective

Wyrick, John J.; Parra, Michael A.

doi:10.1016/j.bbagrm.2008.07.001

Cited by 57 publications

(55 citation statements)

References 101 publications

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“…As we had previously demonstrated, H2A.X-F expression and protein levels decline substantially after the mid-blastula transition, and the protein is not present in somatic cells (37). Histone H2A and H2B are more labile in nucleosomes in general than H3 and H4, and H2A-H2B post-translational modifications are likely to be more transient (57). These observations in general are strongly consistent with a particularly specific biological function for Npm and H2A arginine methylation in early embryogenesis.…”

Section: Discussionmentioning

confidence: 72%

Protein Arginine Methyltransferase Prmt5-Mep50 Methylates Histones H2A and H4 and the Histone Chaperone Nucleoplasmin in Xenopus laevis Eggs

Wilczek

Chitta

Woo

et al. 2011

Journal of Biological Chemistry

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Background: Histones are specifically modified in the Xenopus egg. Results: A complex of Prmt5 and Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin on an arginine in a conserved motif. Conclusion: Arginine methylation is enriched in the egg and targets chromatin-acting proteins. Significance: Histone arginine methylation probably results in specification of the pluripotent developmental program.

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Section: Discussionmentioning

confidence: 72%

Protein Arginine Methyltransferase Prmt5-Mep50 Methylates Histones H2A and H4 and the Histone Chaperone Nucleoplasmin in Xenopus laevis Eggs

Wilczek

Chitta

Woo

et al. 2011

Journal of Biological Chemistry

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“…The same RHR region (residues [17][18][19] has also been demonstrated to interact with a C-terminal acidic patch of Dot1 methyltransferase, facilitating Dot1-mediated histone H3K79 methylation and telomeric silencing (51). For histone H2B, the N-terminal HBR region KKDGKKRKRSRK associates with DNA, stabilizes nucleosome structure, and silences gene expression (52,53). Methylation of these basic regions may compromise their interaction with protein or DNA binding partners, affecting downstream processes, including transcription (54).…”

Section: Discussionmentioning

confidence: 99%

Mammalian Protein Arginine Methyltransferase 7 (PRMT7) Specifically Targets RXR Sites in Lysine- and Arginine-rich Regions

Feng¹,

Maity

Whitelegge³

et al. 2013

Journal of Biological Chemistry

159

212

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Background: Protein arginine methyltransferase 7 (PRMT7) is associated with various functions and diseases, but its substrate specificity is poorly defined. Results: Insect cell-expressed PRMT7 forms -monomethylarginine residues at basic RXR sequences in peptides and histone H2B. Conclusion: PRMT7 is a type III PRMT with a unique substrate specificity. Significance: Novel post-translational modification sites generated by PRMT7 may regulate biological function.

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“…This is the first work describing H2B acetylation modulation in mammals during a physiological process. Indeed, so far, functional studies on acetylation of H2B have been mostly limited to yeast (reviewed by Wyrick and Parra (2009)). Early biochemical experiments showed that acetylation of the histone H2A-H2B dimer facilitated transcription in vitro (Puerta et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

Spatial Memory Consolidation is Associated with Induction of Several Lysine-Acetyltransferase (Histone Acetyltransferase) Expression Levels and H2B/H4 Acetylation-Dependent Transcriptional Events in the Rat Hippocampus

Bousiges

Vasconcelos

Neidl

et al. 2010

Neuropsychopharmacol

165

142

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Numerous genetic studies have shown that the CREB-binding protein (CBP) is an essential component of long-term memory formation, through its histone acetyltransferase (HAT) function. E1A-binding protein p300 and p300/CBP-associated factor (PCAF) have also recently been involved in memory formation. By contrast, only a few studies have reported on acetylation modifications during memory formation, and it remains unclear as to how the system is regulated during this dynamic phase. We investigated acetylation-dependent events and the expression profiles of these HATs during a hippocampus-dependent task taxing spatial reference memory in the Morris water maze. We found a specific increase in H2B and H4 acetylation in the rat dorsal hippocampus, while spatial memory was being consolidated. This increase correlated with the degree of specific acetylated histones enrichment on some memory/plasticity-related gene promoters. Overall, a global increase in HAT activity was measured during this memory consolidation phase, together with a global increase of CBP, p300, and PCAF expression. Interestingly, these regulations were altered in a model of hippocampal denervation disrupting spatial memory consolidation, making it impossible for the hippocampus to recruit the CBP pathway (CBP regulation and acetylated-H2B-dependent transcription). CBP has long been thought to be present in limited concentrations in the cells. These results show, for the first time, that CBP, p300, and PCAF are dynamically modulated during the establishment of a spatial memory and are likely to contribute to the induction of a specific epigenetic tagging of the genome for hippocampus-dependent (spatial) memory consolidation. These findings suggest the use of HAT-activating molecules in new therapeutic strategies of pathological aging, Alzheimer's disease, and other neurodegenerative disorders.

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The role of histone H2A and H2B post-translational modifications in transcription: A genomic perspective

Cited by 57 publications

References 101 publications

Protein Arginine Methyltransferase Prmt5-Mep50 Methylates Histones H2A and H4 and the Histone Chaperone Nucleoplasmin in Xenopus laevis Eggs

Protein Arginine Methyltransferase Prmt5-Mep50 Methylates Histones H2A and H4 and the Histone Chaperone Nucleoplasmin in Xenopus laevis Eggs

Mammalian Protein Arginine Methyltransferase 7 (PRMT7) Specifically Targets RXR Sites in Lysine- and Arginine-rich Regions

Spatial Memory Consolidation is Associated with Induction of Several Lysine-Acetyltransferase (Histone Acetyltransferase) Expression Levels and H2B/H4 Acetylation-Dependent Transcriptional Events in the Rat Hippocampus

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