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Share and share alike: the role of Tra1 from the SAGA and NuA4 coactivator complexes

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Pages 37-43 | Received 25 Jul 2018, Accepted 24 Sep 2018, Published online: 30 Oct 2018

Figures & data

Figure 1. (a) The domain organization of Tra1. The HEAT domain is split into three subdomains named Finger, Ring and Clasp. The C-terminal FAT, FRB, Kinase and FATC domains are collectively referred to as the Head. Residue numbering is shown for S. cerevisiae Tra1. (b) The structure of Tra1 and its location within the SAGA and NuA4 complexes. Tra1 is shown in cylinders representation and color matched to (a). The 35Å aperture between finger and ring subdomains is highlighted by a double headed arrow. The upper and lower row of panels are related by a 90 degree rotation of each structure about the vertical axis, maintaining the same orientation and coloring of Tra1 within each row. Running left to right, the panels show the structure of isolated Tra1 [Citation11], its position within SAGA [Citation12], and within two different NuA4 reconstructions (negative stain (N.S.) [Citation20] and cryo-EM [Citation21]). The locations of the catalytic SAGA histone acetyltransferase (HAT) and histone deubiquitinase (DUB) modules are indicated. The location of individual NuA4 subunits and its catalytic module (Piccolo HAT) are also indicated.

Figure 1. (a) The domain organization of Tra1. The HEAT domain is split into three subdomains named Finger, Ring and Clasp. The C-terminal FAT, FRB, Kinase and FATC domains are collectively referred to as the Head. Residue numbering is shown for S. cerevisiae Tra1. (b) The structure of Tra1 and its location within the SAGA and NuA4 complexes. Tra1 is shown in cylinders representation and color matched to (a). The 35Å aperture between finger and ring subdomains is highlighted by a double headed arrow. The upper and lower row of panels are related by a 90 degree rotation of each structure about the vertical axis, maintaining the same orientation and coloring of Tra1 within each row. Running left to right, the panels show the structure of isolated Tra1 [Citation11], its position within SAGA [Citation12], and within two different NuA4 reconstructions (negative stain (N.S.) [Citation20] and cryo-EM [Citation21]). The locations of the catalytic SAGA histone acetyltransferase (HAT) and histone deubiquitinase (DUB) modules are indicated. The location of individual NuA4 subunits and its catalytic module (Piccolo HAT) are also indicated.