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Histone demethylases and control of gene expression in plants.
Cell Mol Biol (Noisy-le-grand). 2014 Dec 24; 60(5):97-105.CM

Abstract

Covalent histone modifications, chromatin remodeling and incorporation of histone variants regulate the dynamics of chromatin structure. Among covalent histone modifications, histone methylation mediates by histone methylases that influence the gene expression in heterochromatin silencing, genomic imprinting and transcription. In contrast to methylases, histone demethylases remove the methyl groups from lysine or arginine residues of histones and have enormous impact on gene expression via modified chromatin structures. Two types of histone lysie demethylases have been identified, including lysine specific demethylases 1 (LSD1) and Jmj (Jumonji) domain containing family proteins. The human demethyliminase (PADI4) converts monomethyl arginine residue to citrulline by the arginine demethylimination. In this review we summarize recent advances to understand the mechanism of demethylases in regulation of plant gene expression. In addition we are highlighting the function of four human like LSD1 (LDL) and jmj domain containing genes of Arabidopsis that regulate the defense related, flowering controlling and brassinosteroid response genes.

Authors+Show Affiliations

University of Warwick Synthetic Biology, School of life science Coventry United Kingdom.National Research Center on Equines Haryana India.Fox Chase Cancer Center Philadelphia USA lodhiniraj@gmail.com.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

25535719

Citation

Prakash, S, et al. "Histone Demethylases and Control of Gene Expression in Plants." Cellular and Molecular Biology (Noisy-le-Grand, France), vol. 60, no. 5, 2014, pp. 97-105.
Prakash S, Singh R, Lodhi N. Histone demethylases and control of gene expression in plants. Cell Mol Biol (Noisy-le-grand). 2014;60(5):97-105.
Prakash, S., Singh, R., & Lodhi, N. (2014). Histone demethylases and control of gene expression in plants. Cellular and Molecular Biology (Noisy-le-Grand, France), 60(5), 97-105.
Prakash S, Singh R, Lodhi N. Histone Demethylases and Control of Gene Expression in Plants. Cell Mol Biol (Noisy-le-grand). 2014 Dec 24;60(5):97-105. PubMed PMID: 25535719.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Histone demethylases and control of gene expression in plants. AU - Prakash,S, AU - Singh,R, AU - Lodhi,N, Y1 - 2014/12/24/ PY - 2014/07/08/received PY - 2014/07/15/accepted PY - 2014/12/24/entrez PY - 2014/12/24/pubmed PY - 2016/2/24/medline SP - 97 EP - 105 JF - Cellular and molecular biology (Noisy-le-Grand, France) JO - Cell Mol Biol (Noisy-le-grand) VL - 60 IS - 5 N2 - Covalent histone modifications, chromatin remodeling and incorporation of histone variants regulate the dynamics of chromatin structure. Among covalent histone modifications, histone methylation mediates by histone methylases that influence the gene expression in heterochromatin silencing, genomic imprinting and transcription. In contrast to methylases, histone demethylases remove the methyl groups from lysine or arginine residues of histones and have enormous impact on gene expression via modified chromatin structures. Two types of histone lysie demethylases have been identified, including lysine specific demethylases 1 (LSD1) and Jmj (Jumonji) domain containing family proteins. The human demethyliminase (PADI4) converts monomethyl arginine residue to citrulline by the arginine demethylimination. In this review we summarize recent advances to understand the mechanism of demethylases in regulation of plant gene expression. In addition we are highlighting the function of four human like LSD1 (LDL) and jmj domain containing genes of Arabidopsis that regulate the defense related, flowering controlling and brassinosteroid response genes. SN - 1165-158X UR - https://www.unboundmedicine.com/medline/citation/25535719/Histone_demethylases_and_control_of_gene_expression_in_plants_ L2 - http://www.arabidopsis.org/servlets/TairObject?type=publication&id=501762258 DB - PRIME DP - Unbound Medicine ER -