Birck C, Poch O, Romier C, Ruff M, Mengus G, Lavigne A C, Davidson I, Moras D
Institut de Génétique et de Biologie, Moléculaire et Cellulaire, CNRS/INSERM/ULP, Illkirch, C.U. de Strasbourg, France.
Cell. 1998 Jul 24;94(2):239-49. doi: 10.1016/s0092-8674(00)81423-3.
Determination of the crystal structure of the human TBP-associated factor (hTAF(II))28/hTAF(II)18 heterodimer shows that these TAF(II)s form a novel histone-like pair in the TFIID complex. The histone folds in hTAF(II)28 and hTAF(II)18 were not predicted from their primary sequence, indicating that these TAF(II)s define a novel family of atypical histone fold sequences. The TAF(II)18 and TAF(II)28 histone fold motifs are also present in the N- and C-terminal regions of the SPT3 proteins, suggesting that the histone fold in SPT3 may be reconstituted by intramolecular rather than classical intermolecular interactions. The existence of additional histone-like pairs in both the TFIID and SAGA complexes shows that the histone fold is a more commonly used motif for mediating TAF-TAF interactions than previously believed.
人TBP相关因子（hTAF(II)）28/hTAF(II)18异二聚体晶体结构的测定表明，这些TAF(II)在TFIID复合物中形成了一对新型的类组蛋白结构。hTAF(II)28和hTAF(II)18中的组蛋白折叠结构并非由其一级序列预测而来，这表明这些TAF(II)定义了一个非典型组蛋白折叠序列的新家族。TAF(II)18和TAF(II)28组蛋白折叠基序也存在于SPT3蛋白的N端和C端区域，这表明SPT3中的组蛋白折叠可能是通过分子内而非经典的分子间相互作用重新构建的。TFIID和SAGA复合物中都存在额外的类组蛋白对，这表明组蛋白折叠是一种比以前认为的更常用于介导TAF-TAF相互作用的基序。
