 |
PDBsum entry 2j04
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transcription
|
PDB id
|
|
|
|
2j04
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structure of the tau60/delta tau91 subcomplex of yeast transcription factor iiic: insights into preinitiation complex assembly.
|
|
|
Authors
|
|
A.Mylona,
C.Fernández-Tornero,
P.Legrand,
M.Haupt,
A.Sentenac,
J.Acker,
C.W.Müller.
|
|
|
Ref.
|
|
Mol Cell, 2006,
24,
221-232.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Yeast RNA polymerase III is recruited upon binding of subcomplexes tauA and tauB
of transcription factor IIIC (TFIIIC) to the A and B blocks of tRNA gene
promoters. The tauB subcomplex consists of subunits tau60, tau91, and tau138. We
determined the 3.2 A crystal structure of tau60 bound to a large C-terminal
fragment of tau91 (Deltatau91). Deltatau91 protein contains a seven-bladed
propeller preceded by an N-terminal extension, whereas tau60 contains a
structurally homologous propeller followed by a C-terminal domain with a novel
alpha/beta fold. The two propeller domains do not have any detectable DNA
binding activity and mediate heterodimer formation that may serve as scaffold
for tau138 assembly. We show that the C-terminal tau60 domain interacts with the
TATA binding protein (TBP). Recombinant tauB recruits TBP and stimulates
TFIIIB-directed transcription on a TATA box containing tRNA gene, implying a
combined contribution of tauA and tauB to preinitiation complex formation.
|
|
|
|
|
|
|
|
Figure 1.
Figure 1. Crystal Structure of the Yeast τ60/Δτ91 Complex
(A) Ribbon representation of the τ60/Δτ91 complex. The
N-terminal extension and the β propeller of Δτ91 are depicted
in gold and blue, respectively. In τ60, β propeller and
C-terminal domain are depicted in red and green, respectively.
In Δτ91, the disordered loop BC in blade 1 and loop CD in
blade 6 are depicted as dashed lines.
(B) Orthogonal view
of the τ60/Δτ91 complex.
Figures 1, 2A, 2C, and 3A were
generated with the program PyMOL (DeLano, 2002).
|
|
Figure 3.
Figure 3. The τ60/Δτ91 Interface
(A) Stereo diagram
of the interactions between τ60 and Δτ91. The view
corresponds to Figure 1A. Hydrogen bonds are indicated as dashed
lines. Blades and strands involved in the interactions are
indicated for both proteins.
(B) Summary of the
interactions between τ60 and Δτ91. Strands, labeled from A to
D, are represented by arrows. Hydrophobic, polar, basic, and
acidic residues are in green, orange, blue, and red,
respectively. Polar interactions involving main chain atoms are
indicated as dashed gray lines, polar interactions between side
chain atoms as gray lines, and hydrophobic interactions as green
lines. The blades are labeled for both proteins.
(C)
Conservation and electrostatic surface potentials of the τ60
and Δτ91 contact surfaces. The left and right panels show
charge distribution (top) and sequence conservation (bottom) of
the τ60 and Δτ91 contact surfaces, respectively. Sequence
conservation above 70% is depicted in green based on a sequence
alignment of different fungal orthologs (Figures S1 and S2).
Dashed yellow lines indicate interacting regions. Regions of
negative and positive surface potential are depicted in red and
blue, respectively. Figures 3C and 4C were generated with the
program GRASP (Nicholls et al., 1993).
|
|
|
|
|
|
The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2006,
24,
221-232)
copyright 2006.
|
|
|
|
|
|
|
