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Information about Histone Acetylation

Histone Acetyltransferase 1
Identifiers
SymbolHAT1
Entrez8520
HUGO4821
OMIM603053
RefSeqNM_003642
UniProtO14929
Other data
EC number2.3.1.48
LocusChr. 2 q31.2-33.1
Histone acetyltransferases (HAT) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring an acetyl group from acetyl CoA to lysine to form ε-N-acetyl lysine.

Histone acetylation is generally linked to transcriptional activation. These are generally associated with euchromatin. Initially, it was thought that acetylation of lysine neutralizes the positive charge normally present, thus reducing affinity between histone and (negatively charged) DNA which renders DNA more accessible to transcription factors. More recently, it has emerged that lysine acetylation and other posttranslational modifications of histones generate binding sites for specific protein-protein interaction domains, such as the acetyl-lysine binding bromodomain.

Interaction with HDACs

Histone acetyltransferases (HATs) and histone deacetylases (HDACs) are recruited to their target promoters through a physical interaction with a sequence-specific transcription factor (TF). They usually function within a multimolecular complex ('enzymatic complex'), in which the other subunits are necessary for them to modify nucleosomes around the binding site. These enzymes can also modify factors other than histones (protein X)

See also

External links



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Transferases: acyltransferases (EC 2.3)
2.3.1: other than amino-acyl groups
(mostly acetyltransferases)		N-Acetylglutamate synthase - Choline acetyltransferase - Acetyl-Coenzyme A acetyltransferase - Dihydrolipoyl transacetylase - Acetyl-CoA C-acyltransferase - Beta-galactoside transacetylase - Carnitine O-palmitoyltransferase (CPT1, CPT2) - Acyltransferase like 2 - Chloramphenicol acetyltransferase - Aminolevulinic acid synthase - Beta-ketoacyl-ACP synthase - Glyceronephosphate O-acyltransferase - Lecithin-cholesterol acyltransferase - Histone acetyltransferase (P300/CBP) - Serotonin N-acetyl transferase
2.3.2 - AminoacyltransferasesGamma glutamyl transpeptidase - Peptidyl transferase - Transglutaminase (Tissue transglutaminase, Keratinocyte transglutaminase, Factor XIII)
2.3.3 - converted into alkyl on transferCitrate synthase - ATP citrate lyase - HMG-CoA synthase
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Swiss-Prot is a manually curated biological database of protein sequences. Swiss-Prot was created in 1986 by Amos Bairoch during his PhD and developed by the Swiss Institute of Bioinformatics and the European Bioinformatics Institute.
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Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme.
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locus (plural loci) is a fixed position on a chromosome, such as the position of a gene or a biomarker (genetic marker). A variant of the DNA sequence at a given locus is called an allele. The ordered list of loci known for a particular genome is called a genetic map.
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Enzymes are proteins that catalyze (i.e. accelerate) chemical reactions.[1] In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, the products.
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Acetylation (or in IUPAC nomenclature ethanoylation) describes a reaction that introduces an acetyl functional group into an organic compound. Deacetylation is the removal of the acetyl group.
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Lysine (abbreviated as Lys or K)[1] is an α-amino acid with the chemical formula HO2CCH(NH2)(CH2)4NH2.
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amino acid is a molecule that contains both amine and carboxyl functional groups. In biochemistry, this term refers to alpha-amino acids with the general formula H2NCHRCOOH, where R is an organic substituent.
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histones are the chief protein components of chromatin. They act as spools around which DNA winds, and they play a role in gene regulation.

Classes

Six major histone classes are known:
* H1 (sometimes called the linker histone; also related to Histone H5.

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acetyl (ethanoyl), is a functional group, the acyl of acetic acid, with chemical formula -COCH3. It is sometimes abbreviated as Ac (not to be confused with the element actinium). The acetyl radical contains a methyl group single-bonded to a carbonyl.
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Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme, notable for its role in the synthesis and oxidization of fatty acids, and the oxidation of pyruvate in the citric acid cycle. It is adapted from cysteamine, pantothenate, and adenosine triphosphate.
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Transcription is the process through which a DNA sequence is enzymatically copied by an RNA polymerase to produce a complementary RNA. So to say, it is the transfer of genetic information from DNA into RNA.
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Flavour in particle physics
 

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Please [improve the article] or discuss this issue on the talk page. This article has been tagged since December 2006.
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Post-translational modification (PTM) is the chemical modification of a protein after its translation. It is one of the later steps in protein biosynthesis for many proteins. A protein (also called a polypeptide) is a chain of amino acids.
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bromodomain is a protein domain that recognizes acetylated lysine residues on the N-terminal tails of histones. This recognition is often a prerequisite for protein-histone association and chromatin remodeling.
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The packaging of the eukaryotic genome into highly condensed chromatin makes it inaccessible to the factors required for gene transcription, DNA replication, recombination and repair.
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Histone deacetylases (HDAC) (EC number 3.5.1) are a class of enzymes that remove acetyl groups from an ε-N-acetyl lysine amino acid on a histone. Its action is opposite to that of histone acetyltransferase.
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Histone methyltransferases (HMT) are enzymes, histone-lysine N-methyltransferase and histone-arginine N-methyltransferase, which catalyze the transfer of one to three methyl groups from the cofactor S-Adenosyl methionine to lysine and arginine residues of histone proteins.
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Acetyltransferase is a type of transferase enzyme which transfers an acetyl group.

Examples include:
  • CBP histone acetyltransferase
  • Choline acetyltransferase
  • Chloramphenicol acetyltransferase
  • Histone acetyltransferase

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Medical Subject Headings (MeSH) is a huge controlled vocabulary (or metadata system) for the purpose of indexing journal articles and books in the life sciences. Created and updated by the United States National Library of Medicine (NLM), it is used by the MEDLINE/PubMed
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In biochemistry, a transferase is an enzyme that catalyzes the transfer of a functional group (e.g. a methyl or phosphate group) from one molecule (called the donor) to another (called the acceptor).
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Acyltransferase is a type of transferase enzyme which acts upon acyl groups.

Examples include:
  • Glyceronephosphate O-acyltransferase
  • Lecithin-cholesterol acyltransferase

See also

  • Acetyltransferase

External links


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Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme.
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Acetyltransferase is a type of transferase enzyme which transfers an acetyl group.

Examples include:
  • CBP histone acetyltransferase
  • Choline acetyltransferase
  • Chloramphenicol acetyltransferase
  • Histone acetyltransferase

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N-acetylglutamate synthase is an enzyme which catalyses the production of N-acetylglutamate from acetyl-CoA and glutamate.

This enzyme is important in bacteria and plants for the synthesis of arginine, because it is part of this pathway.
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Choline acetyltransferase (EC 2.3.1.6 ) is an enzyme which is synthesized within the body of a neuron. It is then transferred to the nerve terminal via axoplasmic flow. It joins Acetyl CoA to choline, resulting in the formation of the neurotransmitter acetylcholine.
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