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GNAT family

The GNAT family is related to GCN5 acetyltransferases that are represented in mammals by two closely related proteins, GCN5 and p300/CREB-binding... [Pg.264]

The structures of four HATs (yeast Hatl, Gcn5 from yeast (y) and Tetrahymena thermophUa (t), human PCAF, yeast Hpa2) from the GNAT family have been solved so far [15-19]. These structures show that the evolutionarily conserved sequences of these proteins - termed motifs A, B, C, D [14] - form a conserved structural core. This core domain is constituted by a central highly curved five-stranded... [Pg.24]

Binding of Histone Substrates by HATs of the GNAT Family... [Pg.27]

Structure of a HAT from the p300/CBP family has been long awaited, since these enzymes have no sequence similarity with enzymes of the GNAT and MYST families. The structure of the p300 HAT domain was solved very recently in complex with a Lys-GoA bi-substrate inhibitor, which required a highly intricate expression and purification protocol in order to produce a protein amenable to crystallization studies [24]. Analysis of the structure revealed however that, despite no sequence conservation, a similar structural core is observed as for the GNAT and MYST... [Pg.26]

Histone acetyltransferase (HAT) enzymes are divided into several families based on conserved sequence motifs. The two major families are named GNAT (Gcn5-related... [Pg.73]

See other pages where GNAT family is mentioned: [Pg.246]    [Pg.353]    [Pg.354]    [Pg.24]    [Pg.26]    [Pg.27]    [Pg.29]    [Pg.248]    [Pg.466]    [Pg.691]    [Pg.695]    [Pg.246]    [Pg.353]    [Pg.354]    [Pg.24]    [Pg.26]    [Pg.27]    [Pg.29]    [Pg.248]    [Pg.466]    [Pg.691]    [Pg.695]    [Pg.232]    [Pg.297]    [Pg.398]    [Pg.130]    [Pg.6]    [Pg.24]    [Pg.27]    [Pg.29]    [Pg.74]    [Pg.464]    [Pg.29]    [Pg.386]    [Pg.321]    [Pg.296]    [Pg.160]    [Pg.69]   
See also in sourсe #XX -- [ Pg.246 ]

See also in sourсe #XX -- [ Pg.266 , Pg.355 , Pg.356 ]

See also in sourсe #XX -- [ Pg.24 , Pg.73 , Pg.242 ]



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GNAT

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