Molecular Basis for the Recognition of Phosphorylated and Phosphoacetylated Histone H3 by 14-3-3

MacDonald, Neil; Welburn, Julie; Noble, M.E.M.; Nguyen, Anhco; Yaffe, Michael B.; Clynes, David; Moggs, Jonathan G.; Orphanides, George M.; Thomson, Stuart; Edmunds, John; Clayton, Alison L.; Endicott, Jane; Mahadevan, Louis C.

doi:10.1016/j.molcel.2005.08.032

Cited by 219 publications

(215 citation statements)

References 61 publications

(76 reference statements)

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“…Pull-downs with H3S28ph showed higher enrichments of 14-3-3 proteins than H3S10ph, which is consistent with previous reports. 12 −14 None of the phosphorylated threonine residues mediated binding of the 14-3-3 proteins, although 14-3-3 proteins are known to bind such phosphorylation sites as well. The second amino acid downstream of the phosphorylation site (P + 2) is critical in most 14-3-3 binding sites, and Figure 2.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Analysis of Phosphorylation-Dependent Protein–Protein Interactions of Histone H3

Klingberg¹,

Jost

Schümann³

et al. 2014

ACS Chem. Biol.

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Multiple posttranslational modifications (PTMs) of histone proteins including site-specific phosphorylation of serine and threonine residues govern the accessibility of chromatin. According to the histone code theory, PTMs recruit regulatory proteins or block their access to chromatin. Here, we report a general strategy for simultaneous analysis of both of these effects based on a SILAC MS scheme. We applied this approach for studying the biochemical role of phosphorylated S10 of histone H3. Differential pull-down experiments with H3-tails synthesized from L-and D-amino acids uncovered that histone acetyltransferase 1 (HAT1) and retinoblastoma-binding protein 7 (RBBP7) are part of the protein network, which interacts with the unmodified H3-tail. An additional H3-derived bait containing the nonhydrolyzable phospho-serine mimic phosphonomethylenalanine (Pma) at S10 recruited several isoforms of the 14-3-3 family and blocked the recruitment of HAT1 and RBBP7 to the unmodified H3-tail. Our observations provide new insights into the many functions of H3S10 phosphorylation. In addition, the outlined methodology is generally applicable for studying specific binding partners of unmodified histone tails.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Analysis of Phosphorylation-Dependent Protein–Protein Interactions of Histone H3

Klingberg¹,

Jost

Schümann³

et al. 2014

ACS Chem. Biol.

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“…This modification is recognized by the 14-3-3ζ protein, a member of the 14-3-3 protein family [76]. Furthermore, studies in Drosophila melanogaster have indicated that this protein family is involved in recruiting components of the elongation complex to chromatin [77].…”

Section: Regulating the Binding Of Chromatin Factorsmentioning

confidence: 99%

Regulation of chromatin by histone modifications

2011

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Chromatin is not an inert structure, but rather an instructive DNA scaffold that can respond to external cues to regulate the many uses of DNA. A principle component of chromatin that plays a key role in this regulation is the modification of histones. There is an ever-growing list of these modifications and the complexity of their action is only just beginning to be understood. However, it is clear that histone modifications play fundamental roles in most biological processes that are involved in the manipulation and expression of DNA. Here, we describe the known histone modifications, define where they are found genomically and discuss some of their functional consequences, concentrating mostly on transcription where the majority of characterisation has taken place.

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“…6(G)]. 72 The jumonji domain of JHDM3A (JMJD2A) catalyzes the demethylation of di-and tri-methylated Lys10 and Lys 37 in histone H3 [ Fig. 6(H)].…”

Section: Examination Of the Morfs In Rnap II And Histone H3mentioning

confidence: 99%

Exploring the binding diversity of intrinsically disordered proteins involved in one‐to‐many binding

et al. 2013

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Molecular recognition features (MoRFs) are intrinsically disordered protein regions that bind to partners via disorder-to-order transitions. In one-to-many binding, a single MoRF binds to two or more different partners individually. MoRF-based one-to-many protein-protein interaction (PPI) examples were collected from the Protein Data Bank, yielding 23 MoRFs bound to 2-9 partners, with all pairs of same-MoRF partners having less than 25% sequence identity. Of these, 8 MoRFs were bound to 2-9 partners having completely different folds, whereas 15 MoRFs were bound to 2-5 partners having the same folds but with low sequence identities. For both types of partner variation, backbone and side chain torsion angle rotations were used to bring about the conformational changes needed to enable close fits between a single MoRF and distinct partners. Alternative splicing events (ASEs) and posttranslational modifications (PTMs) were also found to contribute to distinct partner binding. Because ASEs and PTMs both commonly occur in disordered regions, and because both ASEs and PTMs are often tissue-specific, these data suggest that MoRFs, ASEs, and PTMs may collaborate to alter PPI networks in different cell types. These data enlarge the set of carefully studied MoRFs that use inherent flexibility and that also use ASE-based and/or PTM-based surface modifications to enable the same disordered segment to selectively associate with two or more partners. The small number of residues involved in MoRFs and in their modifications by ASEs or PTMs may simplify the evolvability of signaling network diversity.

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Molecular Basis for the Recognition of Phosphorylated and Phosphoacetylated Histone H3 by 14-3-3

Cited by 219 publications

References 61 publications

Analysis of Phosphorylation-Dependent Protein–Protein Interactions of Histone H3

Analysis of Phosphorylation-Dependent Protein–Protein Interactions of Histone H3

Regulation of chromatin by histone modifications

Exploring the binding diversity of intrinsically disordered proteins involved in one‐to‐many binding

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