InterPro : IPR005910

Name  Histone acetyltransferase ELP3 Short Name  Hist_AcTrfase_ELP3
Type  Family Description  Histone acetylation is carried out by a class of enzymes known as histone acetyltransferases(HATs), which catalyse the transfer of an acetyl group from acetyl-CoA to the lysine E-aminogroups on the N-terminal tails of histones []. Early indication that HATs were involved in transcriptioncame from the observation that in actively transcribed regions of chromatin, histones tend to behyperacetylated, whereas in transcriptionally silent regions histones are hypoacetylated. The histone acetyltransferases are divided into five families. These include the Gcn5-relatedacetyltransferases (GNATs); the MYST (for `MOZ, Ybf2/Sas3, Sas2 and Tip60)-related HATs;p300/CBP HATs; the general transcription factor HATs, which include the TFIID subunit TAF250;and the nuclear hormone-related HATs SRC1 and ACTR (SRC3).The GCN5-related N-acetyltransferase superfamily includes such enzymes as the histone acetyltransferases GCN5 and Hat1, the elongator complex subunit Elp3,the mediator-complex subunit Nut1, and Hpa2 [].Many GNATs share several functional domains, including an N-terminal region of variable length, anacetyltransferase domain that encompasses the conserved sequence motifs described above, aregion that interacts with the coactivator Ada2, and a C-terminal bromodomain that is believed tointeract with acetyl-lysine residues. Members of the GNAT family are important for the regulation of cell growth and development. Inmice, knockouts of Gcn5L are embryonic lethal. Yeast Gcn5 is needed for normal progressionthrough the G2-M boundary and mitotic gene expression. The importance of GNATs isprobably related to their role in transcription and DNA repair.The yeast GCN5 (yGCN5) transcriptional coactivator functions as a histone acetyltransferase (HAT) to promote transcriptional activation. The crystal structure of the yeast histone acetyltransferase Hat1-acetyl coenzyme A (AcCoA) shows that Hat1 has an elongated, curved structure, and the AcCoA molecule is bound in a cleft on the concave surface of the protein, marking the active site of the enzyme. A channel of variable width and depth that runs across the protein is probably the binding site for the histone substrate []. The central protein core associated with AcCoA binding that appears to be structurally conserved among a superfamily of N-acetyltransferases, including yeast histone acetyltransferase 1 and Serratia marcescensaminoglycoside 3-N-acetyltransferase [].The Saccharomyces cerevisiae(Baker's yeast) member YPL086C has been characterised in vitro as an N-terminal acetyltransferase () for all four core histones. It is a component of the RNA polymerase II holoenzyme, designated Elp3p for Elongator Protein 3. Members of this family are found in eukaryotes and archaea. These proteins are part of the larger set of GNAT acetyltransferases. In vivo, ELP3 gene deletion confers typical ELP phenotypes such as slow growth adaptation, slow gene activation, and temperature sensitivity. This suggests a role for the proteins as novel, tightly RNAPII-associated histone acetyltransferases in transcription of DNA packaged in chromatin [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

2 Contains

Id Name Short Name Type
IPR000182 GNAT domain GNAT_dom Domain
IPR006638 Elongator protein 3/MiaB/NifB Elp3/MiaB/NifB Domain

0 Found In

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Neuwald AF GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. 1997 Trends Biochem Sci 22 154-5
Dutnall RN Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. 1998 Cell 94 427-38
Trievel RC Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. 1999 Proc Natl Acad Sci U S A 96 8931-6
Wittschieben BO A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme. 1999 Mol Cell 4 123-8
Carrozza MJ The diverse functions of histone acetyltransferase complexes. 2003 Trends Genet 19 321-9

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)