Mass Spectrometric Mapping of Linker Histone H1 Variants Reveals Multiple Acetylations, Methylations, and Phosphorylation as Well as Differences between Cell Culture and Tissue

Wiśniewski, Jacek R.; Zougman, Alexandre; Krüger, Sonja; Mann, Matthias

doi:10.1074/mcp.m600255-mcp200

Cited by 222 publications

(367 citation statements)

References 57 publications

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“…However, H1 is also modified on other residues (Wisniewski et al 2007;Zheng et al 2010;and others), and those modifications might act synergistically. Further studies will be needed to unravel the crosstalk between different linker histone modifications as well as their interdependence with core histone modifications.…”

Section: Discussionmentioning

confidence: 99%

“…The purification of endogenous GCN5-containing SAGA and ATAC complexes from HeLa cells was as described previously (Nagy et al 2009(Nagy et al , 2010. Histone H1 extraction with perchloric acid (PCA) was performed as described previously (Wisniewski et al 2007). The ChIP protocol and ChIP-seq data analysis are described in detail in the Supplemental Material.…”

Section: Methodsmentioning

confidence: 99%

“…S1B, bottom). Interestingly, this residue is acetylated in vivo (Wisniewski et al 2007). We therefore raised an antibody for H1.4K34 acetylation (H1.4K34ac).…”

Section: H14k34 Is Modified By Acetylationmentioning

confidence: 99%

“…In particular, the acetylation of lysine residues on core histone tails has been linked with transcription (Allfrey et al 1964;Kurdistani and Grunstein 2003) by either a direct effect on chromatin structure (e.g., as shown for H4K16 acetylation) (Robinson et al 2008) or the recruitment of effector bromodomain-containing proteins (Yang 2004). The linker histone H1 has been shown to be also acetylated in vivo (Garcia et al 2004;Vaquero et al 2004;Wisniewski et al 2007), but this modification has not been functionally characterized.…”

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confidence: 99%

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A dual role of linker histone H1.4 Lys 34 acetylation in transcriptional activation

Kamieniarz¹,

Izzo²,

Dundr³

et al. 2012

Genes Dev.

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The linker histone H1 is a key player in chromatin organization, yet our understanding of the regulation of H1 functions by post-translational modifications is very limited. We provide here the first functional characterization of H1 acetylation. We show that H1.4K34 acetylation (H1.4K34ac) is mediated by GCN5 and is preferentially enriched at promoters of active genes, where it stimulates transcription by increasing H1 mobility and recruiting a general transcription factor. H1.4K34ac is dynamic during spermatogenesis and marks undifferentiated cells such as induced pluripotent stem (iPS) cells and testicular germ cell tumors. We propose a model for H1.4K34ac as a novel regulator of chromatin function with a dual role in transcriptional activation.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

“…S1B, bottom). Interestingly, this residue is acetylated in vivo (Wisniewski et al 2007). We therefore raised an antibody for H1.4K34 acetylation (H1.4K34ac).…”

Section: H14k34 Is Modified By Acetylationmentioning

confidence: 99%

mentioning

confidence: 99%

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A dual role of linker histone H1.4 Lys 34 acetylation in transcriptional activation

Kamieniarz¹,

Izzo²,

Dundr³

et al. 2012

Genes Dev.

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“…In addition to the microheterogeneity of H1 histones, they can also be posttranslationally modified in various ways (16). Phosphorylation is believed to be the most vital modification.…”

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confidence: 99%

Translocation of histone H1 subtypes between chromatin and cytoplasm during mitosis in normal human fibroblasts

et al. 2010

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Histone H1 is an important constituent of chromatin, which undergoes major structural rearrangements during mitosis. However, the role of H1, multiple H1 subtypes, and H1 phosphorylation is still unclear. In normal human fibroblasts, phosphorylated H1 was found located in nuclei during prophase and in both cytoplasm and condensed chromosomes during metaphase, anaphase, and telophase as detected by immunocytochemistry. Moreover, we detected remarkable differences in the distribution of the histone H1 subtypes H1.2, H1.3, and H1.5 during mitosis. H1.2 was found in chromatin during prophase and almost solely in the cytoplasm of metaphase and early anaphase cells. In late anaphase, it appeared in both chromatin and cytoplasm and again in chromatin during telophase. H1.5 distribution pattern resembled that of H1.2, but H1.5 was partitioned between chromatin and cytoplasm during metaphase and early anaphase. H1.3 was detected in chromatin in all cell cycle phases. We propose therefore, that H1 subtype translocation during mitosis is controlled by phosphorylation, in combination with H1 subtype inherent affinity. We conclude that H1 subtypes, or their phosphorylated forms, may leave chromatin in a regulated way to give access for chromatin condensing factors or transcriptional regulators during mitosis. ' 2010International Society for Advancement of Cytometry Key terms histone H1; chromatin; cell cycle; mitosis IN the cell cycle, DNA and protein content are duplicated, and the cell divides in two in a strict sequential order of events. During prophase, the replicated chromosomes condense, and the nuclear membrane breaks down in prometaphase. At metaphase, the chromosomes are aligned at the equator of the mitotic spindle, and the sister chromatids are segregated to the two poles of the spindle during anaphase. Finally, the separation is completed during telophase by cytoplasmic division. Impaired cell cycle control or cell cycle progression may result in cell death or malignant transformation.

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Histones: Gene Organisation and Post‐translational Modification

Doenecke

2014

Encyclopedia of Life Sciences

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Histones are highly conserved basic proteins that form the major part of the protein moiety of eukaryotic chromosomes. Together with deoxyribonucleic acid (DNA) , they organise the repeat unit of chromatin, the nucleosome, which consists of a deoxyribonucleoprotein core particle and linker DNA connecting these core units. The core particle is composed of 147 nucleotide pairs of DNA and two copies of each of the four core histones H2A, H2B, H3 and H4. The DNA linking core particles is associated with one copy of a fifth histone type termed H1. The basal organisation of chromatin as a histone–DNA complex implies that histones functionally participate in the regulation of chromatin‐bound processes, such as transcription, DNA repair or DNA replication. Post‐translational modification of histone amino acid side chains or replacement of canonical histones by nonallelic variants and recognition of such modified sites by regulatory factors are key processes in modulating the functional organisation of chromatin. Key Concepts: The histone family of basic chromosome consists of five protein classes that organise together with DNA the nucleosome, the basic chromatin unit. Two copies of each of the four histones H2A, H2B, H3 and H4 form together with DNA the nucleosome core particle; linker DNA and histone H1 complete the nucleosome as the chromosomal repeat unit. The five canonical histones are extremely conserved proteins, and the nucleosome structure is essentially the same from unicellular to vertebrate species. Nonallelic variants of four of the five histones (the exception is H4) can replace the canonical isoforms, thereby mediating dynamic changes of chromatin structure and function. Histones are post‐translationally modified by, for example, acetylation of lysine residues, methylation of lysine or arginine residues and phosphorylation of hydroxyl groups in side chains of serine, threonine or tyrosine. Such modified side chains (and combinations thereof) provide interaction sites for binding of factors involved in chromatin‐bound processes. Histone H1 is also termed linker histones, because it interacts with the DNA linking nucleosome core particles. Yeast has just one type of H1‐like histones, whereas mammals have several nonallelic H1 variants. H1 is involved in the formation of higher order chromatin structures above the level of arrays of nucleosomes.

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Mass Spectrometric Mapping of Linker Histone H1 Variants Reveals Multiple Acetylations, Methylations, and Phosphorylation as Well as Differences between Cell Culture and Tissue

Cited by 222 publications

References 57 publications

A dual role of linker histone H1.4 Lys 34 acetylation in transcriptional activation

A dual role of linker histone H1.4 Lys 34 acetylation in transcriptional activation

Translocation of histone H1 subtypes between chromatin and cytoplasm during mitosis in normal human fibroblasts

Histones: Gene Organisation and Post‐translational Modification

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