Chromatin and Aging

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Abstract

Recent studies from a number of model organisms have indicated chromatin structure and its remodeling as a major contributory agent for aging. Few recent experiments also demonstrate that modulation in the chromatin modifying agents also affect the life span of an organism and even in some cases the change is inherited epigenetically to subsequent generations. Hence, in the present report we discuss the chromatin organization and its changes during aging.

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Most cited references 147

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The biology of chromatin remodeling complexes.

Cedric R Clapier, Bradley Cairns (2009)

The packaging of chromosomal DNA by nucleosomes condenses and organizes the genome, but occludes many regulatory DNA elements. However, this constraint also allows nucleosomes and other chromatin components to actively participate in the regulation of transcription, chromosome segregation, DNA replication, and DNA repair. To enable dynamic access to packaged DNA and to tailor nucleosome composition in chromosomal regions, cells have evolved a set of specialized chromatin remodeling complexes (remodelers). Remodelers use the energy of ATP hydrolysis to move, destabilize, eject, or restructure nucleosomes. Here, we address many aspects of remodeler biology: their targeting, mechanism, regulation, shared and unique properties, and specialization for particular biological processes. We also address roles for remodelers in development, cancer, and human syndromes.

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Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain.

A Bannister, P Zegerman, J F Partridge … (2001)

Heterochromatin protein 1 (HP1) is localized at heterochromatin sites where it mediates gene silencing. The chromo domain of HP1 is necessary for both targeting and transcriptional repression. In the fission yeast Schizosaccharomyces pombe, the correct localization of Swi6 (the HP1 equivalent) depends on Clr4, a homologue of the mammalian SUV39H1 histone methylase. Both Clr4 and SUV39H1 methylate specifically lysine 9 of histone H3 (ref. 6). Here we show that HP1 can bind with high affinity to histone H3 methylated at lysine 9 but not at lysine 4. The chromo domain of HP1 is identified as its methyl-lysine-binding domain. A point mutation in the chromo domain, which destroys the gene silencing activity of HP1 in Drosophila, abolishes methyl-lysine-binding activity. Genetic and biochemical analysis in S. pombe shows that the methylase activity of Clr4 is necessary for the correct localization of Swi6 at centromeric heterochromatin and for gene silencing. These results provide a stepwise model for the formation of a transcriptionally silent heterochromatin: SUV39H1 places a 'methyl marker' on histone H3, which is then recognized by HP1 through its chromo domain. This model may also explain the stable inheritance of the heterochromatic state.

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Histone H4-K16 acetylation controls chromatin structure and protein interactions.

Michael A. Shogren-Knaak, Haruhiko Ishii, Jian-Min Sun … (2006)

Acetylation of histone H4 on lysine 16 (H4-K16Ac) is a prevalent and reversible posttranslational chromatin modification in eukaryotes. To characterize the structural and functional role of this mark, we used a native chemical ligation strategy to generate histone H4 that was homogeneously acetylated at K16. The incorporation of this modified histone into nucleosomal arrays inhibits the formation of compact 30-nanometer-like fibers and impedes the ability of chromatin to form cross-fiber interactions. H4-K16Ac also inhibits the ability of the adenosine triphosphate-utilizing chromatin assembly and remodeling enzyme ACF to mobilize a mononucleosome, indicating that this single histone modification modulates both higher order chromatin structure and functional interactions between a nonhistone protein and the chromatin fiber.

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Author and article information

Contributors

Pramod C. Rath: pramod.rath@gmail.com

Ramesh Sharma: +919103642722113 , sharamesh@gmail.com

S. Prasad: +919105426702517 , +919105422368174 , s.sprasadbhu@gmail.com

Madan Mohan Chaturvedi: +91-11-27666702 , mchaturvedi@zoology.du.ac.in , director@cic.du.ac.in

Journal

Journal ID (publisher-id): 978-981-10-2155-8

Journal ID (doi): 10.1007/978-981-10-2155-8

Journal ID (nlm-ta): Topics in Biomedical Gerontology

Title: Topics in Biomedical Gerontology

ISBN (Print): 978-981-10-2154-1

ISBN (Electronic): 978-981-10-2155-8

Publication date (Electronic): 18 August 2016

Pages: 205-241

Affiliations

[1 ]GRID grid.10706.30, ISNI 000000040498924X, School of Life Sciences, Molecular Biology Laboratory, , Jawaharlal Nehru University, ; New Delhi, Delhi India

[2 ]GRID grid.412227.0, ISNI 000000012173057X, Department of Biochemistry, , North Eastern Hill University, ; Shillong, Megalaya India

[3 ]GRID grid.411507.6, ISNI 0000000122878816, Biochemistry & Molecular Biology Lab, Department of Zoology, , Banaras Hindu University, ; Varanasi, Uttar Pradesh India

[4 ]GRID grid.8195.5, ISNI 0000000121094999, Cluster Innovation Centre, University Stadium, , Delhi University, ; Sports Complex, G.C. Narang Marg, North Campus, Delhi, 110007 India

[5 ]GRID grid.8195.5, ISNI 0000000121094999, Laboratory for Chromatin Biology, Department of Zoology, , University of Delhi, ; Room no. 317, 2nd Floor, North Campus, Delhi, 110007 India

Article

Publisher ID: 11

DOI: 10.1007/978-981-10-2155-8_11

PMC ID: 7121440

SO-VID: 3ae4c70b-a968-4835-80fa-b06e7c1c67da

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This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.

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Keywords: histone modification,chromatin structure,core histone,chromatin domain,rdna region

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Keywords: histone modification, chromatin structure, core histone, chromatin domain, rdna region

Chromatin and Aging

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Abstract

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Higher order chromatin architecture

Most cited references 147

The biology of chromatin remodeling complexes.

Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain.

Histone H4-K16 acetylation controls chromatin structure and protein interactions.

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