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  1. Article: Characterizing metabolic drivers of

    Bustin, Katelyn A / Abbas, Arwa / Wang, Xie / Abt, Michael C / Zackular, Joseph P / Matthews, Megan L

    Frontiers in pharmacology

    2023  Volume 14, Page(s) 1074619

    Abstract: Many enzymes require post-translational modifications or cofactor machinery for primary function. As these catalytically essential moieties are highly regulated, they act as dual sensors and chemical handles for context-dependent metabolic activity. ...

    Abstract Many enzymes require post-translational modifications or cofactor machinery for primary function. As these catalytically essential moieties are highly regulated, they act as dual sensors and chemical handles for context-dependent metabolic activity.
    Language English
    Publishing date 2023-01-26
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587355-6
    ISSN 1663-9812
    ISSN 1663-9812
    DOI 10.3389/fphar.2023.1074619
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  2. Article ; Online: Biological Functions of HMGN Chromosomal Proteins.

    Nanduri, Ravikanth / Furusawa, Takashi / Bustin, Michael

    International journal of molecular sciences

    2020  Volume 21, Issue 2

    Abstract: Chromatin plays a key role in regulating gene expression programs necessary for the orderly progress of development and for preventing changes in cell identity that can lead to disease. The high mobility group N (HMGN) is a family of nucleosome binding ... ...

    Abstract Chromatin plays a key role in regulating gene expression programs necessary for the orderly progress of development and for preventing changes in cell identity that can lead to disease. The high mobility group N (HMGN) is a family of nucleosome binding proteins that preferentially binds to chromatin regulatory sites including enhancers and promoters. HMGN proteins are ubiquitously expressed in all vertebrate cells potentially affecting chromatin function and epigenetic regulation in multiple cell types. Here, we review studies aimed at elucidating the biological function of HMGN proteins, focusing on their possible role in vertebrate development and the etiology of disease. The data indicate that changes in HMGN levels lead to cell type-specific phenotypes, suggesting that HMGN optimize epigenetic processes necessary for maintaining cell identity and for proper execution of specific cellular functions. This manuscript contains tables that can be used as a comprehensive resource for all the English written manuscripts describing research aimed at elucidating the biological function of the HMGN protein family.
    MeSH term(s) Animals ; Chromatin ; Disease ; Epigenesis, Genetic ; Gene Expression Regulation, Developmental ; HMGN Proteins ; High Mobility Group Proteins/classification ; High Mobility Group Proteins/genetics ; High Mobility Group Proteins/physiology ; Humans ; Mice ; Promoter Regions, Genetic
    Chemical Substances Chromatin ; HMGN Proteins ; High Mobility Group Proteins
    Language English
    Publishing date 2020-01-10
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms21020449
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  3. Article ; Online: H3K27ac nucleosomes facilitate HMGN localization at regulatory sites to modulate chromatin binding of transcription factors.

    Zhang, Shaofei / Postnikov, Yuri / Lobanov, Alexei / Furusawa, Takashi / Deng, Tao / Bustin, Michael

    Communications biology

    2022  Volume 5, Issue 1, Page(s) 159

    Abstract: Nucleosomes containing acetylated H3K27 are a major epigenetic mark of active chromatin and identify cell-type specific chromatin regulatory regions which serve as binding sites for transcription factors. Here we show that the ubiquitous nucleosome ... ...

    Abstract Nucleosomes containing acetylated H3K27 are a major epigenetic mark of active chromatin and identify cell-type specific chromatin regulatory regions which serve as binding sites for transcription factors. Here we show that the ubiquitous nucleosome binding proteins HMGN1 and HMGN2 bind preferentially to H3K27ac nucleosomes at cell-type specific chromatin regulatory regions. HMGNs bind directly to the acetylated nucleosome; the H3K27ac residue and linker DNA facilitate the preferential binding of HMGNs to the modified nucleosomes. Loss of HMGNs increases the levels of H3K27me3 and the histone H1 occupancy at enhancers and promoters and alters the interaction of transcription factors with chromatin. These experiments indicate that the H3K27ac epigenetic mark enhances the interaction of architectural protein with chromatin regulatory sites and identify determinants that facilitate the localization of HMGN proteins at regulatory sites to modulate cell-type specific gene expression.
    MeSH term(s) Chromatin/genetics ; HMGN Proteins/chemistry ; HMGN Proteins/genetics ; HMGN Proteins/metabolism ; Nucleosomes/genetics ; Protein Binding ; Transcription Factors/genetics ; Transcription Factors/metabolism
    Chemical Substances Chromatin ; HMGN Proteins ; Nucleosomes ; Transcription Factors
    Language English
    Publishing date 2022-02-23
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-022-03099-0
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  4. Article: High mobility group proteins.

    Bustin, Michael

    Biochimica et biophysica acta

    2010  Volume 1799, Issue 1-2, Page(s) 1–2

    MeSH term(s) Animals ; Chromatin/metabolism ; Disease ; Epigenesis, Genetic ; High Mobility Group Proteins/metabolism ; Histones/metabolism ; Humans
    Chemical Substances Chromatin ; High Mobility Group Proteins ; Histones
    Language English
    Publishing date 2010-01
    Publishing country Netherlands
    Document type Editorial ; Introductory Journal Article
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbagrm.2010.01.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Nongenetic functions of the genome.

    Bustin, Michael / Misteli, Tom

    Science (New York, N.Y.)

    2016  Volume 352, Issue 6286, Page(s) aad6933

    Abstract: The primary function of the genome is to store, propagate, and express the genetic information that gives rise to a cell's architectural and functional machinery. However, the genome is also a major structural component of the cell. Besides its genetic ... ...

    Abstract The primary function of the genome is to store, propagate, and express the genetic information that gives rise to a cell's architectural and functional machinery. However, the genome is also a major structural component of the cell. Besides its genetic roles, the genome affects cellular functions by nongenetic means through its physical and structural properties, particularly by exerting mechanical forces and by serving as a scaffold for binding of cellular components. Major cellular processes affected by nongenetic functions of the genome include establishment of nuclear structure, signal transduction, mechanoresponses, cell migration, and vision in nocturnal animals. We discuss the concept, mechanisms, and implications of nongenetic functions of the genome.
    MeSH term(s) Animals ; Cell Movement ; Cell Nucleus/chemistry ; Cell Nucleus/metabolism ; Cell Nucleus/ultrastructure ; DNA/chemistry ; DNA/ultrastructure ; DNA Damage ; Genome/genetics ; Genome/physiology ; Humans ; Mechanotransduction, Cellular ; Nucleic Acid Conformation ; Signal Transduction ; Stress, Mechanical
    Chemical Substances DNA (9007-49-2)
    Language English
    Publishing date 2016-05-05
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.aad6933
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  6. Article ; Online: H3K27ac nucleosomes facilitate HMGN localization at regulatory sites to modulate chromatin binding of transcription factors

    Shaofei Zhang / Yuri Postnikov / Alexei Lobanov / Takashi Furusawa / Tao Deng / Michael Bustin

    Communications Biology, Vol 5, Iss 1, Pp 1-

    2022  Volume 14

    Abstract: The nucleosome-binding proteins HMGN1 and HMGN2 prefer acetylated nucleosomes at H3K27ac and the loss of this interaction alters binding of transcription factors to chromatin. ...

    Abstract The nucleosome-binding proteins HMGN1 and HMGN2 prefer acetylated nucleosomes at H3K27ac and the loss of this interaction alters binding of transcription factors to chromatin.
    Keywords Biology (General) ; QH301-705.5
    Language English
    Publishing date 2022-02-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Biological Functions of HMGN Chromosomal Proteins

    Ravikanth Nanduri / Takashi Furusawa / Michael Bustin

    International Journal of Molecular Sciences, Vol 21, Iss 2, p

    2020  Volume 449

    Abstract: Chromatin plays a key role in regulating gene expression programs necessary for the orderly progress of development and for preventing changes in cell identity that can lead to disease. The high mobility group N (HMGN) is a family of nucleosome binding ... ...

    Abstract Chromatin plays a key role in regulating gene expression programs necessary for the orderly progress of development and for preventing changes in cell identity that can lead to disease. The high mobility group N (HMGN) is a family of nucleosome binding proteins that preferentially binds to chromatin regulatory sites including enhancers and promoters. HMGN proteins are ubiquitously expressed in all vertebrate cells potentially affecting chromatin function and epigenetic regulation in multiple cell types. Here, we review studies aimed at elucidating the biological function of HMGN proteins, focusing on their possible role in vertebrate development and the etiology of disease. The data indicate that changes in HMGN levels lead to cell type-specific phenotypes, suggesting that HMGN optimize epigenetic processes necessary for maintaining cell identity and for proper execution of specific cellular functions. This manuscript contains tables that can be used as a comprehensive resource for all the English written manuscripts describing research aimed at elucidating the biological function of the HMGN protein family.
    Keywords hmgn proteins ; chromatin ; epigenetics ; gene regulation ; development ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 612
    Language English
    Publishing date 2020-01-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Multiple epigenetic factors co-localize with HMGN proteins in A-compartment chromatin.

    He, Bing / Zhu, Iris / Postnikov, Yuri / Furusawa, Takashi / Jenkins, Lisa / Nanduri, Ravikanth / Bustin, Michael / Landsman, David

    Epigenetics & chromatin

    2022  Volume 15, Issue 1, Page(s) 23

    Abstract: Background: Nucleosomal binding proteins, HMGN, is a family of chromatin architectural proteins that are expressed in all vertebrate nuclei. Although previous studies have discovered that HMGN proteins have important roles in gene regulation and ... ...

    Abstract Background: Nucleosomal binding proteins, HMGN, is a family of chromatin architectural proteins that are expressed in all vertebrate nuclei. Although previous studies have discovered that HMGN proteins have important roles in gene regulation and chromatin accessibility, whether and how HMGN proteins affect higher order chromatin status remains unknown.
    Results: We examined the roles that HMGN1 and HMGN2 proteins play in higher order chromatin structures in three different cell types. We interrogated data generated in situ, using several techniques, including Hi-C, Promoter Capture Hi-C, ChIP-seq, and ChIP-MS. Our results show that HMGN proteins occupy the A compartment in the 3D nucleus space. In particular, HMGN proteins occupy genomic regions involved in cell-type-specific long-range promoter-enhancer interactions. Interestingly, depletion of HMGN proteins in the three different cell types does not cause structural changes in higher order chromatin, i.e., in topologically associated domains (TADs) and in A/B compartment scores. Using ChIP-seq combined with mass spectrometry, we discovered protein partners that are directly associated with or neighbors of HMGNs on nucleosomes.
    Conclusions: We determined how HMGN chromatin architectural proteins are positioned within a 3D nucleus space, including the identification of their binding partners in mononucleosomes. Our research indicates that HMGN proteins localize to active chromatin compartments but do not have major effects on 3D higher order chromatin structure and that their binding to chromatin is not dependent on specific protein partners.
    MeSH term(s) Chromatin ; Epigenesis, Genetic ; HMGN Proteins/chemistry ; HMGN Proteins/genetics ; HMGN Proteins/metabolism ; Nucleosomes ; Protein Binding
    Chemical Substances Chromatin ; HMGN Proteins ; Nucleosomes
    Language English
    Publishing date 2022-06-27
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, N.I.H., Extramural
    ZDB-ID 2462129-8
    ISSN 1756-8935 ; 1756-8935
    ISSN (online) 1756-8935
    ISSN 1756-8935
    DOI 10.1186/s13072-022-00457-4
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  9. Article: Functional interplay between histone H1 and HMG proteins in chromatin.

    Postnikov, Yuri V / Bustin, Michael

    Biochimica et biophysica acta

    2015  Volume 1859, Issue 3, Page(s) 462–467

    Abstract: The dynamic interaction of nucleosome binding proteins with their chromatin targets is an important element in regulating the structure and function of chromatin. Histone H1 variants and High Mobility Group (HMG) proteins are ubiquitously expressed in ... ...

    Abstract The dynamic interaction of nucleosome binding proteins with their chromatin targets is an important element in regulating the structure and function of chromatin. Histone H1 variants and High Mobility Group (HMG) proteins are ubiquitously expressed in all vertebrate cells, bind dynamically to chromatin, and are known to affect chromatin condensation and the ability of regulatory factors to access their genomic binding sites. Here, we review the studies that focus on the interactions between H1 and HMGs and highlight the functional consequences of the interplay between these architectural chromatin binding proteins. H1 and HMG proteins are mobile molecules that bind to nucleosomes as members of a dynamic protein network. All HMGs compete with H1 for chromatin binding sites, in a dose dependent fashion, but each HMG family has specific effects on the interaction of H1 with chromatin. The interplay between H1 and HMGs affects chromatin organization and plays a role in epigenetic regulation.
    MeSH term(s) Animals ; Carrier Proteins/physiology ; Chromatin/chemistry ; High Mobility Group Proteins/physiology ; Histones/physiology ; Humans
    Chemical Substances Carrier Proteins ; Chromatin ; High Mobility Group Proteins ; Histones
    Language English
    Publishing date 2015-10-08
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbagrm.2015.10.006
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  10. Article ; Online: Epigenetic regulation of white adipose tissue plasticity and energy metabolism by nucleosome binding HMGN proteins.

    Nanduri, Ravikanth / Furusawa, Takashi / Lobanov, Alexei / He, Bing / Xie, Carol / Dadkhah, Kimia / Kelly, Michael C / Gavrilova, Oksana / Gonzalez, Frank J / Bustin, Michael

    Nature communications

    2022  Volume 13, Issue 1, Page(s) 7303

    Abstract: White adipose tissue browning is a key metabolic process controlled by epigenetic factors that facilitate changes in gene expression leading to altered cell identity. We find that male mice lacking the nucleosome binding proteins HMGN1 and HMGN2 (DKO ... ...

    Abstract White adipose tissue browning is a key metabolic process controlled by epigenetic factors that facilitate changes in gene expression leading to altered cell identity. We find that male mice lacking the nucleosome binding proteins HMGN1 and HMGN2 (DKO mice), show decreased body weight and inguinal WAT mass, but elevated food intake, WAT browning and energy expenditure. DKO white preadipocytes show reduced chromatin accessibility and lower FRA2 and JUN binding at Pparγ and Pparα promoters. White preadipocytes and mouse embryonic fibroblasts from DKO mice show enhanced rate of differentiation into brown-like adipocytes. Differentiating DKO adipocytes show reduced H3K27ac levels at white adipocyte-specific enhancers but elevated H3K27ac levels at brown adipocyte-specific enhancers, suggesting a faster rate of change in cell identity, from white to brown-like adipocytes. Thus, HMGN proteins function as epigenetic factors that stabilize white adipocyte cell identity, thereby modulating the rate of white adipose tissue browning and affecting energy metabolism in mice.
    MeSH term(s) Male ; Animals ; Mice ; Nucleosomes/metabolism ; Adipose Tissue, Brown/metabolism ; HMGN Proteins/metabolism ; Epigenesis, Genetic ; Fibroblasts/metabolism ; Adipose Tissue, White/metabolism ; Adipocytes, Brown/metabolism ; Energy Metabolism/genetics
    Chemical Substances Nucleosomes ; HMGN Proteins
    Language English
    Publishing date 2022-11-26
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-022-34964-5
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