Histone 2B can be modified by the attachment of ubiquitin

West, Michael H. P.; Bonner, William M.

doi:10.1093/nar/8.20.4671

Cited by 232 publications

(146 citation statements)

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“…It is widely distributed in animals, plants, yeasts and bacteria [1,2]. In animal cells ubiquitin has been found both in free form [1,4] or covalently bound by its carboxyl terminal to other proteins [5][6][7][8]. In the chromatin of interphase cells, ~10% of histone 2A and -,-1% of histone 2B are covalently linked to ubiquitin [8].…”

Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

“…In animal cells ubiquitin has been found both in free form [1,4] or covalently bound by its carboxyl terminal to other proteins [5][6][7][8]. In the chromatin of interphase cells, ~10% of histone 2A and -,-1% of histone 2B are covalently linked to ubiquitin [8]. Since the H2A-ubiquitin conjugate, protein A24, is absent from metaphase chromosomes, it has been suggested that ubiquitin plays a role in the cell cycle [9,10].…”

Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

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Formation of conjugates by ¹²⁵I‐labelled ubiquitin microinjected into cultured hepatoma cells

Atidia

Kulka

1982

FEBS Letters

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Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

Formation of conjugates by ¹²⁵I‐labelled ubiquitin microinjected into cultured hepatoma cells

Atidia

Kulka

1982

FEBS Letters

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“…Monoubiquitylated histone H2B: from general to highly specific transcription regulator Ubiquitylation of histone H2B in mammalian cells was identified over three decades ago [37], but more than two decades passed before the function of this modification in regulating mammalian chromatin-associated processes was deciphered. The first breakthrough came with the identification of the budding yeast protein Bre1 [38,39], which, together with the ubiquitin-conjugating enzyme Rad6, serves as the E3 ligase in the monoubiquitylation of the yeast histone H2B on lysine 123 (K123) within transcribed chromatin [38][39][40][41].…”

Section: Open Access Under CC By-nc-nd Licensementioning

confidence: 99%

RNF20–RNF40: A ubiquitin‐driven link between gene expression and the DNA damage response

et al. 2011

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a b s t r a c tThe DNA damage response (DDR) is emerging as a vast signaling network that temporarily modulates numerous aspects of cellular metabolism in the face of DNA lesions, especially critical ones such as the double strand break (DSB). The DDR involves extensive dynamics of protein post-translational modifications, most notably phosphorylation and ubiquitylation. The DSB response is mobilized primarily by the ATM protein kinase, which phosphorylates a plethora of key players in its various branches. It is based on a core of proteins dedicated to the damage response, and a cadre of proteins borrowed temporarily from other cellular processes to help meet the challenge. A recently identified novel component of the DDR pathway -histone H2B monoubiquitylationexemplifies this principle. In mammalian cells, H2B monoubiquitylation is driven primarily by an E3 ubiquitin ligase composed of the two RING finger proteins RNF20 and RNF40. Generation of monoubiquitylated histone H2B (H2Bub) has been known to be coupled to gene transcription, presumably modulating chromatin decondensation at transcribed regions. New evidence indicates that the regulatory function of H2Bub on gene expression can selectively enhance or suppress the expression of distinct subsets of genes through a mechanism involving the hPAF1 complex and the TFIIS protein. This delicate regulatory process specifically affects genes that control cell growth and genome stability, and places RNF20 and RNF40 in the realm of tumor suppressor proteins. In parallel, it was found that following DSB induction, the H2B monoubiquitylation module is recruited to damage sites where it induces local H2Bub, which in turn is required for timely recruitment of DSB repair protein and, subsequently, timely DSB repair. This pathway represents a crossroads of the DDR and chromatin organization, and is a typical example of how the DDR calls to action functional modules that in unprovoked cells regulate other processes. Ó 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. The DNA damage response: borrowing functional modules in an emergencyCellular metabolism is controlled by numerous, interlocked signaling networks. These networks are constantly responding to internal and external stimuli related to the cell's normal life cycle and functions, and to threats to its well being. A major threat to cellular homeostasis is subversion of its genomic stability, which may lead to undue cell death or to neoplasia [1,2]. DNA damage caused by internal or external damaging agents is a major danger to the integrity of the cellular genome. The cellular defense system against this threat is the DNA damage response (DDR) -an elaborate signaling network activated by DNA damage, which swiftly modulates many physiological processes [3,4]. A strong trigger of the DDR is the DNA double-strand break (DSB) [5,6]. DSBs are induced by ionizing radiation, radiomimetic chemicals, reactive oxygen species formed in the course of normal metabolism, and can also result from replic...

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“…About 5-15 % and 1-2 % of histones H2A and H2B, respectively, are ubiquitinated (Robzyk et al 2000;West and Bonner 1980). Histones H3 and H1 are also targets for ubiquitination, but the abundance of ubiquitination marks in these histones is low (Chen et al 1998;Pham and Sauer 2000).…”

Section: Ubiquitination and Sumoylation Of Histonesmentioning

confidence: 99%

Nutrition, Histone Epigenetic Marks, and Disease

Zempleni

Liu

Xue

2013

Environmental Epigenomics in Health and Disease

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The dietary intake of essential nutrients and bioactive food compounds is a process that occurs on a daily basis for the entire life span. Therefore, your diet has a great potential to cause changes in the epigenome. Known histone modifications include acetylation, methylation, biotinylation, poly(ADP-ribosylation), ubiquitination, and sumoylation. Some of these modifications depend directly on dietary nutrients. For other modifications, bioactive dietary compounds may alter the activities of enzymes that establish or remove histone marks, thereby altering the epigenome. This chapter provides an overview of diet-dependent epigenomic marks in histones and their links with human health.

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Histone 2B can be modified by the attachment of ubiquitin

Cited by 232 publications

References 5 publications

Formation of conjugates by ¹²⁵I‐labelled ubiquitin microinjected into cultured hepatoma cells

Formation of conjugates by ¹²⁵I‐labelled ubiquitin microinjected into cultured hepatoma cells

RNF20–RNF40: A ubiquitin‐driven link between gene expression and the DNA damage response

Nutrition, Histone Epigenetic Marks, and Disease

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Histone 2B can be modified by the attachment of ubiquitin

Cited by 232 publications

References 5 publications

Formation of conjugates by 125I‐labelled ubiquitin microinjected into cultured hepatoma cells

Formation of conjugates by 125I‐labelled ubiquitin microinjected into cultured hepatoma cells

RNF20–RNF40: A ubiquitin‐driven link between gene expression and the DNA damage response

Nutrition, Histone Epigenetic Marks, and Disease

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Formation of conjugates by ¹²⁵I‐labelled ubiquitin microinjected into cultured hepatoma cells

Formation of conjugates by ¹²⁵I‐labelled ubiquitin microinjected into cultured hepatoma cells