Translating the Histone Code
Chromatin, the physiological template of all eukaryotic genetic information, is subject to a diverse array of posttranslational modifications that largely impinge on histone amino termini, thereby regulating access to the underlying DNA. Distinct histone amino-terminal modifications can generate syn...
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Published in | Science (American Association for the Advancement of Science) Vol. 293; no. 5532; pp. 1074 - 1080 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
American Society for the Advancement of Science
10.08.2001
American Association for the Advancement of Science The American Association for the Advancement of Science |
Subjects | |
Online Access | Get full text |
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Abstract | Chromatin, the physiological template of all eukaryotic genetic information, is subject to a diverse array of posttranslational modifications that largely impinge on histone amino termini, thereby regulating access to the underlying DNA. Distinct histone amino-terminal modifications can generate synergistic or antagonistic interaction affinities for chromatin-associated proteins, which in turn dictate dynamic transitions between transcriptionally active or transcriptionally silent chromatin states. The combinatorial nature of histone amino-terminal modifications thus reveals a "histone code" that considerably extends the information potential of the genetic code. We propose that this epigenetic marking system represents a fundamental regulatory mechanism that has an impact on most, if not all, chromatin-templated processes, with far-reaching consequences for cell fate decisions and both normal and pathological development. |
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AbstractList | Chromatin, the physiological template of all eukaryotic genetic information, is subject to a diverse array of posttranslational modifications that largely impinge on histone amino termini, thereby regulating access to the underlying DNA. Distinct histone amino-terminal modifications can generate synergistic or antagonistic interaction affinities for chromatin-associated proteins, which in turn dictate dynamic transitions between transcriptionally active or transcriptionally silent chromatin states. The combinatorial nature of histone amino-terminal modifications thus reveals a "histone code" that considerably extends the information potential of the genetic code. We propose that this epigenetic marking system represents a fundamental regulatory mechanism that has an impact on most, if not all, chromatin-templated processes, with far-reaching consequences for cell fate decisions and both normal and pathological development. The combinatorial nature of histone amino-terminal modifications reveals a "histone code" that considerably extends the information potential of the genetic code. Jenuwein and Allis propose that this epigenetic marking system represents a fundamental regulatory mechanism that has an impact on most, if not all, chromatin-templated processes, with far-reaching consequences for cell fate decisions and both normal and pathological development. Chromatin, the physiological template of all eukaryotic genetic information, is subject to a diverse array of posttranslational modifications that largely impinge on histone amino termini, thereby regulating access to the underlying DNA. Distinct histone amino-terminal modifications can generate synergistic or antagonistic interaction affinities for chromatin-associated proteins, which in turn dictate dynamic transitions between transcriptionally active or transcriptionally silent chromatin states. The combinatorial nature of histone amino-terminal modifications thus reveals a "histone code" that considerably extends the information potential of the genetic code. We propose that this epigenetic marking system represents a fundamental regulatory mechanism that has an impact on most, if not all, chromatin-templated processes, with far-reaching consequences for cell fate decisions and both normal and pathological development.Chromatin, the physiological template of all eukaryotic genetic information, is subject to a diverse array of posttranslational modifications that largely impinge on histone amino termini, thereby regulating access to the underlying DNA. Distinct histone amino-terminal modifications can generate synergistic or antagonistic interaction affinities for chromatin-associated proteins, which in turn dictate dynamic transitions between transcriptionally active or transcriptionally silent chromatin states. The combinatorial nature of histone amino-terminal modifications thus reveals a "histone code" that considerably extends the information potential of the genetic code. We propose that this epigenetic marking system represents a fundamental regulatory mechanism that has an impact on most, if not all, chromatin-templated processes, with far-reaching consequences for cell fate decisions and both normal and pathological development. |
Audience | Academic |
Author | Jenuwein, Thomas Allis, C. David |
Author_xml | – sequence: 1 givenname: Thomas surname: Jenuwein fullname: Jenuwein, Thomas – sequence: 2 givenname: C. David surname: Allis fullname: Allis, C. David |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/11498575$$D View this record in MEDLINE/PubMed |
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Snippet | Chromatin, the physiological template of all eukaryotic genetic information, is subject to a diverse array of posttranslational modifications that largely... The combinatorial nature of histone amino-terminal modifications reveals a "histone code" that considerably extends the information potential of the genetic... |
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SubjectTerms | Acetylation Amino Acid Sequence Animals Cells Cells (Biology) Chromatin Chromatin - chemistry Chromatin - metabolism Chromatin - ultrastructure Coding Deoxyribonucleic acid DNA Double stranded RNA Epigenetics Eukaryotes Eukaryotic cells Evidence Gene Expression Regulation Gene Silencing Genes Genetic aspects Genetic code Genetics Genomic Imprinting Genomics Heredity Histones Histones - chemistry Histones - genetics Histones - metabolism Individualized Instruction Information Storage Methylation Molecular Sequence Data Nucleosomes Phosphorylation Protein Structure, Tertiary Proteins Stem cells Transcription, Genetic Transcriptional Activation Viewpoints and Reviews |
Title | Translating the Histone Code |
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