SET domain proteins modulate chromatin domains in eu- and heterochromatin

@article{Jenuwein1998SETDP,
  title={SET domain proteins modulate chromatin domains in eu- and heterochromatin},
  author={Thomas Jenuwein and G{\"o}tz Laible and Rainer Dorn and Gunter Reuter},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={1998},
  volume={54},
  pages={80-93}
}
Abstract. 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… 
The Arabidopsis SUVR4 protein is a nucleolar histone methyltransferase with preference for monomethylated H3K9
TLDR
The closely related SUVR1, SUVR2 and SUVR4 proteins contain a novel domain at their N-terminus, and a SUVR specific region preceding the SET domain, suggesting involvement in regulation of rRNA expression, in contrast to other SET-domain proteins studied so far.
Molecular genetic analysis of the Drosophila trithorax-related gene which encodes a novel SET domain protein
The Arabidopsis SUVR 4 protein is a nucleolar histone methyltransferase with preference for monomethylated H 3 K 9
TLDR
The closely related SUVR1, SUVR2 and SUVR4 proteins contain a novel domain at their N-terminus, and a SUVR specific region preceding the SET domain, suggesting involvement in regulation of rRNA expression, in contrast to other SET-domain proteins studied so far.
Bacterial SET domain proteins and their role in eukaryotic chromatin modification
TLDR
The hypothesis that SET domain genes found in extant bacteria are of bacterial origin is argued in favor and the available information on pathogen and symbiont SET-domain containing proteins and their targets in eukaryotic organisms is focused on.
Gene expression pattern Molecular genetic analysis of the Drosophila trithorax-relatedgene which encodes a novel SET domain protein
TLDR
The cloning and characterization of a new gene, trithorax-related (trr), is reported, which shares sequence similarities with members of both the trith orax and Polycomb groups and is most similar in sequence to the human ALR protein, suggesting that trr is a Drosophila homologue of the ALR.
Chromatin silencing and activation by Polycomb and trithorax group proteins
TLDR
The study of the evolutionarily conserved PcG/trxG factors has recently gained additional urgency with the realization that they play a pertinent role in certain human cancers.
A Motif within SET-Domain Proteins Binds Single-Stranded Nucleic Acids and Transcribed and Supercoiled DNAs and Can Interfere with Assembly of Nucleosomes
TLDR
It is suggested that the motifs described here may be directly involved in the biological function(s) of SET-containing proteins, and might play a role in the initial recruitment of the proteins to target genes, in the maintenance of their association after DNA replication, or in sustaining DNA stretches in a single-stranded configuration to allow for continuous transcription.
Self-association of the SET domains of human ALL-1 and of Drosophila TRITHORAX and ASH1 proteins
TLDR
Yeast two hybrid methodology, in vivo immunoprecipitation and in vitro `pull down' techniques are applied to show self association of the SET motifs of ALL-1, TRITHORAX and ASH1 proteins (Drosophila AsH1 is encoded by a trithorax-group gene).
The enhancer of polycomb gene of Drosophila encodes a chromatin protein conserved in yeast and mammals.
TLDR
The occurrence of E(Pc) across such divergent species is unusual for both PcG proteins and for suppressors of position-effect variegation, and suggests that E(pc) has an important role in the regulation of chromatin structure in eukaryotes.
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Analysis of yeast SET1, a yeast member of the trithorax gene family that was identified by sequence inspection to encode a 1080-amino acid protein with a C-terminal SET domain, suggests that yeast SET2, like its SET domain counterparts in other organisms, functions in diverse biological processes including transcription and chromatin structure.
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