Chromatin modifications by methylation and ubiquitination: implications in the regulation of gene expression.
It is more evident now than ever that nucleosomes can transmit epigenetic information from one cell generation to the next. It has been demonstrated during the past decade that the posttranslational modifications of histone proteins within the chromosome impact chromatin structure, gene transcription, and epigenetic information. Multiple modifications decorate each histone tail within the nucleosome, including some amino acids that can be modified in several different ways. Covalent modifications of histone tails known thus far include acetylation, phosphorylation, sumoylation, ubiquitination, and methylation. A large body of experimental evidence compiled during the past several years has demonstrated the impact of histone acetylation on transcriptional control. Although histone modification by methylation and ubiquitination was discovered long ago, it was only recently that functional roles for these modifications in transcriptional regulation began to surface. Highlighted in this review are the recent biochemical, molecular, cellular, and physiological functions of histone methylation and ubiquitination involved in the regulation of gene expression as determined by a combination of enzymological, structural, and genetic methodologies.
Shilatifard
Ali
A
Saint Louis University School of Medicine and the Saint Louis University Cancer Center, St. Louis, Missouri 63104, USA. shilatia@slu.edu
D000595:Amino Acid Sequence; D000818:Animals; D002843:Chromatin / Q000235:genetics / Q000378:metabolism*; D005786:Gene Expression Regulation; D020868:Gene Silencing; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000378:metabolism; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D051788:Myeloid-Lymphoid Leukemia Protein / Q000378:metabolism; D063146:Polycomb-Group Proteins; D011499:Protein Processing, Post-Translational; D034622:RNA Interference; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D025801:Ubiquitin / Q000378:metabolism*; D049951:X Chromosome Inactivation
D002843:Chromatin; D006657:Histones; C497422:KMT2A protein, human; D063146:Polycomb-Group Proteins; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D025801:Ubiquitin; D051788:Myeloid-Lymphoid Leukemia Protein; D008780:Methyltransferases; C448996:Set2 protein, S cerevisiae; D011495:Histone-Lysine N-Methyltransferase; D008239:Lysine