High mobility group proteins and their post-translational modifications

Zhang, Qingchun; Wang, Yinsheng

doi:10.1016/j.bbapap.2008.04.028

Cited by 81 publications

(90 citation statements)

References 140 publications

(196 reference statements)

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“…Yet these patterns of phosphorylation are not well studied. The high mobility group proteins exhibit modifications similar to histones and are found in association with histones in chromatin (50). Other examples include tubulin (51) and p53 (52).…”

Section: Discussionmentioning

confidence: 99%

High Throughput Characterization of Combinatorial Histone Codes

Young

DiMaggio

Plazas-Mayorca

et al. 2009

Molecular & Cellular Proteomics

290

357

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We present a novel method utilizing "saltless" pH gradient weak cation exchange-hydrophilic interaction liquid chromatography directly coupled to electron transfer dissociation (ETD) mass spectrometry for the automated on-line high throughput characterization of hypermodified combinatorial histone codes. This technique, performed on a low resolution mass spectrometer, displays an improvement over existing methods with an ϳ100-fold reduction in sample requirements and analysis time. The scheme presented is capable of identifying all of the major combinatorial histone codes present in a sample in a 2-h analysis. The large N-terminal histone peptides are eluted by the pH and organic solvent weak cation exchangehydrophilic interaction liquid chromatography gradient and directly introduced via nanoelectrospray ionization into a benchtop linear quadrupole ion trap mass spectrometer equipped with ETD. Each polypeptide is sequenced, and the modification sites are identified by ETD fragmentation. The isobaric trimethyl and acetyl modifications are resolved chromatographically and confidently distinguished by the synthesis of mass spectrometric and chromatographic information. We demonstrate the utility of the method by complete characterization of human histone H3.2 and histone H4 from butyrate-treated cells, but it is generally applicable to the analysis of highly modified peptides. We find this methodology very useful for chromatographic separation of isomeric species that cannot be separated well by any other chromatographic means, leading to less complicated tandem mass spectra. The improved separation and increased sensitivity generated novel information about much less abundant forms. In this method demonstration we report over 200 H3. Eukaryotic nuclear DNA is nominally compacted into chromatin fibers by use of nucleosomes consisting of a 146-bp section of DNA wrapped around a core of histone proteins (1). Dynamic post-translational modifications (PTMs) 1 of the histones, primarily in the accessible N-terminal region or histone "tail," are an important but not fully understood component of dynamic gene regulation, epigenetic inheritance of cellular memory, genomic stability, and other nuclear mechanisms (2-7). An overwhelming number of studies point to the existence of a histone code of biological logic written on these proteins through these PTMs that are read by a diverse array of "effector" proteins leading to distinct biological events (3). Many single PTM sites on various histone proteins have been decidedly linked to specific physiological processes, such as histone H3 Lys-9 trimethylation (H3K9me3), which is associated with heterochromatin formation (one mode of gene silencing). Nevertheless what effect multiple modifications occurring in combination may have on modulating the histone code signal remains to be determined. Significant progress has been made toward understanding histone modifications using antibody-based histone modification detection methods and by bottom up mass spectrometry (4 -6). However...

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Section: Discussionmentioning

confidence: 99%

High Throughput Characterization of Combinatorial Histone Codes

Young

DiMaggio

Plazas-Mayorca

et al. 2009

Molecular & Cellular Proteomics

290

357

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“…Post-translational modifications of HMG proteins can alter their interactions with DNA and proteins, and consequently, affect their biological activities (1). HMGB1, for example, could be phosphorylated and/or acetylated by pro-inflammatory signals and translocated to the cytoplasm for secretion (12,13) to induce proinflammatory response (14,15).…”

Section: High Mobility Group Nucleosomal Binding Domain 2 (Hmgn2)mentioning

confidence: 99%

“…HMG proteins are subject to a wide range of post-translational modifications including acetylation, methylation, SUMOylation, and phosphorylation (1). Post-translational modifications of HMG proteins can alter their interactions with DNA and proteins, and consequently, affect their biological activities (1).…”

Section: High Mobility Group Nucleosomal Binding Domain 2 (Hmgn2)mentioning

confidence: 99%

“…They have been reported to play important roles in regulating chromatin dynamics, transcriptional activities of genes, and other cellular processes (1)(2)(3). HMG proteins are architectural DNA-and nucleosome-binding proteins subdivided into three families: HMG-AT-hook families (HMGA), HMG-box families (HMGB), and HMG-nucleosome binding families (HMGN), which modulate chromatin structure (4).…”

Section: High Mobility Group Nucleosomal Binding Domain 2 (Hmgn2)mentioning

confidence: 99%

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High Mobility Group Nucleosomal Binding Domain 2 (HMGN2) SUMOylation by the SUMO E3 Ligase PIAS1 Decreases the Binding Affinity to Nucleosome Core Particles

Kim²,

Kwak³

et al. 2014

Journal of Biological Chemistry

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Background: HMGN2 is an important nuclear protein that is involved in altering the chromatin structure and facilitating the transcriptional activation. Results: HMGN2 is modified by SUMO1 with help of E3 ligase PIAS1. Conclusion: HMGN2-SUMOylation is a significant factor in the regulation of chromatin structure and function. Significance: Our finding is the identification of the new modification of HMGN2.

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“…In addition to the shared biochemical properties already noted, the D1 protein is predicted to have extensive intrinsic protein disorder (Uversky et al 2005; data not shown), a demonstrated attribute of HMGA proteins (Lehn et al 1988;Huth et al 1997). Both D1 and HMGA proteins are highly post-translationally modified (Zhai et al 2008;Zhang and Wang 2008). The primary distinction, increased size for D1, is accompanied by a proportional increase in number of AT-hook motifs.…”

Section: Discussionmentioning

confidence: 99%

The Multi-AT-Hook Chromosomal Protein of Drosophila melanogaster, D1, Is Dispensable for Viability

Weiler

Chatterjee

2009

Genetics

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The D1 protein is a high mobility group A (HMGA)-like nonhistone chromosomal protein with primary localization to certain AT-rich satellite DNA sequences within heterochromatin. The binding of D1 to euchromatic sequences is less studied and the functional significance of its chromosomal associations is unclear. By taking advantage of existing P-insertion alleles of the D1 gene, I generated D1 null mutations to investigate the phenotypic effect of loss of the D1 gene. In contrast to a previous report, I determined that the D1 gene is not essential for viability of Drosophila melanogaster, and moreover, that loss of D1 has no obvious phenotypic effects. My tests for an effect of D1 mutations on PEV revealed that it is not a suppressor of variegation, as concluded by other investigators. In fact, the consequence of loss of D1 on one of six variegating rearrangements tested, T(2;3)Sb V , was dominant enhancement of PEV, suggesting a role for the protein in euchromatic chromatin structure and/or transcription. A study of D1 protein sequence conservation highlighted features shared with mammalian HMGA proteins, which function as architectural transcription factors.

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High mobility group proteins and their post-translational modifications

Cited by 81 publications

References 140 publications

High Throughput Characterization of Combinatorial Histone Codes

High Throughput Characterization of Combinatorial Histone Codes

High Mobility Group Nucleosomal Binding Domain 2 (HMGN2) SUMOylation by the SUMO E3 Ligase PIAS1 Decreases the Binding Affinity to Nucleosome Core Particles

The Multi-AT-Hook Chromosomal Protein of Drosophila melanogaster, D1, Is Dispensable for Viability

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