4atg | pdb_00004atg

TAF6 C-terminal domain from Antonospora locustae

spinqualitylabelsall models 4atg, resolution 1.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4atg is a 1 chain structure with sequence from Antonospora locustae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NHE Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The general transcription factor TFIID recognizes specifically the core promoter of genes transcribed by eukaryotic RNA Polymerase II, nucleating the assembly of the pre-initiation complex at the transcription start site. Yet, the understanding in molecular terms of TFIID assembly and function remains poorly understood. Histone fold motifs have been shown to be extremely important for the heterodimerization of many TFIID subunits. However, these subunits display several evolutionary conserved non-canonical features compared to histones, including additional regions whose role is unknown. Here we show that the conserved additional C-terminal region of TFIID subunit TAF6 can be divided into two domains: a small middle domain (TAF6M) and a large C-terminal domain (TAF6C). Our crystal structure of the TAF6C domain from Antonospora locustae at 1.9 A resolution reveals the presence of five conserved HEAT-repeats. Based on these data, we designed several mutants that were introduced into full-length human TAF6. Surprisingly, the mutants affect the interaction between TAF6 and TAF9, suggesting that the formation of the complex between these two TFIID subunits do not only depend on their histone fold motifs. In addition, the same mutants affect even more strongly the interaction between TAF6 and TAF9 in the context of a TAF5/TAF6/TAF9 complex. Expression of these mutants in HeLa cells reveals that most of them are unstable, suggesting their poor incorporation within endogeneous TFIID. Taken together, our results suggest that the conserved additional domains in histone fold-containing subunits of TFIID and of co-activator SAGA are important for the assembly of these complexes. TFIID TAF6/TAF9 complex formation involves the HEAT repeat-containing C-terminal domain of TAF6 and is modulated by TAF5.,Scheer E, Delbac F, Tora L, Moras D, Romier C J Biol Chem. 2012 Jun 13. PMID:22696218 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA