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COMPASS Complex
Introduction Complex Proteins Associated with Set1, also known as COMPASS, is a conserved protein complex playing a major role as a H3K4me3 methylase Methyltransferases are a large group of enzymes that all methylate their substrates but can be split into several subclasses based on their structural features. The most common class of methyltransferases is class I, all of which contain a Rossm ... in eukaryotes. Since it was first identified in 2001, other members of the COMPASS family of methylases with different functions have been discovered, in particular in humans. The Compass complex, or similar protein complexes, have been identified in species ranging from single celled fungi to humans. They play an important regulatory role in many invaluable biological processes including DNA repair, the progression of the cell cycle and transcription through the methylenation of histone lysines. The COMPASS complex is an example of a trithorax-group protein. The MLL1/SET domain ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Set1
Set1 is a gene that codes for Histone-lysine N-methyltransferase and H3 lysine-4 specific proteins ( H3K). Set1 proteins can also be referred to as COMPASS proteins. The first H3K4 methylase, ''Saccharomyces cerevisiae'' Set1/COMPASS, is highly conserved across a multitude of phylogenies. The histone methylation facilitated by Set1 is required for cell growth and transcription silencing through the repression of RNA polymerase II RNA polymerase II (RNAP II and Pol II) is a multiprotein complex that transcribes DNA into precursors of messenger RNA (mRNA) and most small nuclear RNA (snRNA) and microRNA. It is one of the three RNAP enzymes found in the nucleus of eukaryo .... The Set1C, COMPASS Complex, also aids in transcription elongation regulation and the maintenance of telomere length. References Genes {{Gene-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Complex
A protein complex or multiprotein complex is a group of two or more associated polypeptide chains. Protein complexes are distinct from multienzyme complexes, in which multiple catalytic domains are found in a single polypeptide chain. Protein complexes are a form of quaternary structure. Proteins in a protein complex are linked by non-covalent protein–protein interactions. These complexes are a cornerstone of many (if not most) biological processes. The cell is seen to be composed of modular supramolecular complexes, each of which performs an independent, discrete biological function. Through proximity, the speed and selectivity of binding interactions between enzymatic complex and substrates can be vastly improved, leading to higher cellular efficiency. Many of the techniques used to enter cells and isolate proteins are inherently disruptive to such large complexes, complicating the task of determining the components of a complex. Examples of protein complexes include th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
H3K4me3
H3K4me3 is an epigenetic modification to the DNA packaging protein Histone H3 that indicates tri-methylation at the 4th lysine residue of the histone H3 protein and is often involved in the regulation of gene expression. The name denotes the addition of three methyl groups ( trimethylation) to the lysine 4 on the histone H3 protein. H3 is used to package DNA in eukaryotic cells (including human cells), and modifications to the histone alter the accessibility of genes for transcription. H3K4me3 is commonly associated with the activation of transcription of nearby genes. H3K4 trimethylation regulates gene expression through chromatin remodeling by the NURF complex. This makes the DNA in the chromatin more accessible for transcription factors, allowing the genes to be transcribed and expressed in the cell. More specifically, H3K4me3 is found to positively regulate transcription by bringing histone acetylases and nucleosome remodelling enzymes (NURF). H3K4me3 also plays an impo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Methyltransferase
Methyltransferases are a large group of enzymes that all methylate their substrates but can be split into several subclasses based on their structural features. The most common class of methyltransferases is class I, all of which contain a Rossmann fold for binding ''S''-Adenosyl methionine (SAM). Class II methyltransferases contain a SET domain, which are exemplified by SET domain histone methyltransferases, and class III methyltransferases, which are membrane associated. Methyltransferases can also be grouped as different types utilizing different substrates in methyl transfer reactions. These types include protein methyltransferases, DNA/RNA methyltransferases, natural product methyltransferases, and non-SAM dependent methyltransferases. SAM is the classical methyl donor for methyltransferases, however, examples of other methyl donors are seen in nature. The general mechanism for methyl transfer is a SN2-like nucleophilic attack where the methionine sulfur serves as the l ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Eukaryote
Eukaryotes () are organisms whose cells have a nucleus. All animals, plants, fungi, and many unicellular organisms, are Eukaryotes. They belong to the group of organisms Eukaryota or Eukarya, which is one of the three domains of life. Bacteria and Archaea (both prokaryotes) make up the other two domains. The eukaryotes are usually now regarded as having emerged in the Archaea or as a sister of the Asgard archaea. This implies that there are only two domains of life, Bacteria and Archaea, with eukaryotes incorporated among archaea. Eukaryotes represent a small minority of the number of organisms, but, due to their generally much larger size, their collective global biomass is estimated to be about equal to that of prokaryotes. Eukaryotes emerged approximately 2.3–1.8 billion years ago, during the Proterozoic eon, likely as flagellated phagotrophs. Their name comes from the Greek εὖ (''eu'', "well" or "good") and κάρυον (''karyon'', "nut" or "kernel"). E ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Trithorax-group Proteins
Trithorax-group proteins (TrxG) are a heterogeneous collection of proteins whose main action is to maintain gene expression. They can be categorized into three general classes based on molecular function: # histone-modifying TrxG proteins # chromatin-remodeling TrxG proteins # DNA-binding TrxG proteins, plus other TrxG proteins not categorized in the first three classes. Discovery The founding member of TrxG proteins, trithorax (trx), was discovered ~1978 by Philip Ingham as part of his doctoral thesis while a graduate student in the laboratory of J.R.S. Whittle at the University of Sussex. Histone-lysine ''N''-methyltransferase 2A is the human homolog of trx. The table contains names of Drosophila TrxG members. Homologs in other species may have different names. Function Trithorax-group proteins typically function in large complexes formed with other proteins. The complexes formed by TrxG proteins are divided into two groups: histone-modifying complexes and ATP-depend ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
