SET domain proteins modulate chromatin domains in eu- and heterochromatin
The SET domain is a 130-amino acid, evolutionarily conserved sequence motif present in chromosomal proteins that function in modulating gene activities from yeast to mammals. Initially identified as members of the Polycomb- and trithorax-group (Pc-G and trx-G) gene families, which are required to ma...
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| Veröffentlicht in: | Cellular and molecular life sciences : CMLS 1998-01, Vol.54 (1), p.80-93 |
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| creator | Jenuwein, T Laible, G Dorn, R Reuter, G |
| description | The SET domain is a 130-amino acid, evolutionarily conserved sequence motif present in chromosomal proteins that function in modulating gene activities from yeast to mammals. Initially identified as members of the Polycomb- and trithorax-group (Pc-G and trx-G) gene families, which are required to maintain expression boundaries of homeotic selector (HOM-C) genes, SET domain proteins are also involved in position-effect-variegation (PEV), telomeric and centromeric gene silencing, and possibly in determining chromosome architecture. These observations implicate SET domain proteins as multifunctional chromatin regulators with activities in both eu- and heterochromatin--a role consistent with their modular structure, which combines the SET domain with additional sequence motifs of either a cysteine-rich region/zinc-finger type or the chromo domain. Multiple functions for chromatin regulators are not restricted to the SET protein family, since many trx-G (but only very few Pc-G) genes are also modifiers of PEV. Together, these data establish a model in which the modulation of chromatin domains is mechanistically linked with the regulation of key developmental loci (e.g. HOM-C). |
| doi_str_mv | 10.1007/s000180050127 |
| format | Article |
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Initially identified as members of the Polycomb- and trithorax-group (Pc-G and trx-G) gene families, which are required to maintain expression boundaries of homeotic selector (HOM-C) genes, SET domain proteins are also involved in position-effect-variegation (PEV), telomeric and centromeric gene silencing, and possibly in determining chromosome architecture. These observations implicate SET domain proteins as multifunctional chromatin regulators with activities in both eu- and heterochromatin--a role consistent with their modular structure, which combines the SET domain with additional sequence motifs of either a cysteine-rich region/zinc-finger type or the chromo domain. Multiple functions for chromatin regulators are not restricted to the SET protein family, since many trx-G (but only very few Pc-G) genes are also modifiers of PEV. Together, these data establish a model in which the modulation of chromatin domains is mechanistically linked with the regulation of key developmental loci (e.g. HOM-C).</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s000180050127</identifier><identifier>PMID: 9487389</identifier><language>eng</language><publisher>Switzerland: Springer Nature B.V</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Chromatin ; Chromatin - drug effects ; Chromatin - metabolism ; Chromosomal Proteins, Non-Histone ; Chromosomes ; Conserved Sequence ; Gene expression ; Heterochromatin ; Heterochromatin - metabolism ; Molecular biology ; Molecular Sequence Data ; Protein Structure, Tertiary ; Proteins ; Proteins - physiology ; Sequence Homology, Amino Acid ; Suppression, Genetic ; Transcription Factors ; Yeasts</subject><ispartof>Cellular and molecular life sciences : CMLS, 1998-01, Vol.54 (1), p.80-93</ispartof><rights>Birkhäuser Verlag Basel, 1998</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c508t-6c3dfc1345aa7291343cae8634e82382cd4a455466247e2d09a8095e0374230f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11147257/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11147257/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9487389$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jenuwein, T</creatorcontrib><creatorcontrib>Laible, G</creatorcontrib><creatorcontrib>Dorn, R</creatorcontrib><creatorcontrib>Reuter, G</creatorcontrib><title>SET domain proteins modulate chromatin domains in eu- and heterochromatin</title><title>Cellular and molecular life sciences : CMLS</title><addtitle>Cell Mol Life Sci</addtitle><description>The SET domain is a 130-amino acid, evolutionarily conserved sequence motif present in chromosomal proteins that function in modulating gene activities from yeast to mammals. Initially identified as members of the Polycomb- and trithorax-group (Pc-G and trx-G) gene families, which are required to maintain expression boundaries of homeotic selector (HOM-C) genes, SET domain proteins are also involved in position-effect-variegation (PEV), telomeric and centromeric gene silencing, and possibly in determining chromosome architecture. These observations implicate SET domain proteins as multifunctional chromatin regulators with activities in both eu- and heterochromatin--a role consistent with their modular structure, which combines the SET domain with additional sequence motifs of either a cysteine-rich region/zinc-finger type or the chromo domain. Multiple functions for chromatin regulators are not restricted to the SET protein family, since many trx-G (but only very few Pc-G) genes are also modifiers of PEV. Together, these data establish a model in which the modulation of chromatin domains is mechanistically linked with the regulation of key developmental loci (e.g. HOM-C).</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Chromatin</subject><subject>Chromatin - drug effects</subject><subject>Chromatin - metabolism</subject><subject>Chromosomal Proteins, Non-Histone</subject><subject>Chromosomes</subject><subject>Conserved Sequence</subject><subject>Gene expression</subject><subject>Heterochromatin</subject><subject>Heterochromatin - metabolism</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Proteins - physiology</subject><subject>Sequence Homology, Amino Acid</subject><subject>Suppression, Genetic</subject><subject>Transcription 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domain proteins modulate chromatin domains in eu- and heterochromatin</title><author>Jenuwein, T ; Laible, G ; Dorn, R ; Reuter, G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c508t-6c3dfc1345aa7291343cae8634e82382cd4a455466247e2d09a8095e0374230f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Chromatin</topic><topic>Chromatin - drug effects</topic><topic>Chromatin - metabolism</topic><topic>Chromosomal Proteins, Non-Histone</topic><topic>Chromosomes</topic><topic>Conserved Sequence</topic><topic>Gene expression</topic><topic>Heterochromatin</topic><topic>Heterochromatin - metabolism</topic><topic>Molecular biology</topic><topic>Molecular Sequence Data</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Proteins - physiology</topic><topic>Sequence Homology, 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| ispartof | Cellular and molecular life sciences : CMLS, 1998-01, Vol.54 (1), p.80-93 |
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| source | MEDLINE; Springer Nature - Complete Springer Journals; PubMed Central |
| subjects | Amino Acid Sequence Amino acids Animals Chromatin Chromatin - drug effects Chromatin - metabolism Chromosomal Proteins, Non-Histone Chromosomes Conserved Sequence Gene expression Heterochromatin Heterochromatin - metabolism Molecular biology Molecular Sequence Data Protein Structure, Tertiary Proteins Proteins - physiology Sequence Homology, Amino Acid Suppression, Genetic Transcription Factors Yeasts |
| title | SET domain proteins modulate chromatin domains in eu- and heterochromatin |
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