Human TAFII28 and TAFII18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family
Human TAFII28 and TAFII18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family
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DOI：
10.1016/s0092-8674(00)81423-3
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发表时间：
1998-07-24
期刊：
影响因子：
64.5
通讯作者：
Moras, D
中科院分区：
文献类型：
--
作者：
Birck, C;Poch, O;Moras, D
人TAP相关因子（hTAF（II））28/hTAF（II）18异源二聚体的晶体结构的测定表明，这些TAF（II）在TFIID复合物中形成新的组蛋白样对。hTAF（II）28和hTAF（II）18中的组蛋白折叠不能从它们的一级序列预测，表明这些TAF（II）定义了一个新的非典型组蛋白折叠序列家族。TAF（II）18和TAF（II）28组蛋白折叠蛾也存在于SPT 3蛋白的N-和C-末端区域，这表明SPT 3中的组蛋白折叠可以通过分子内而不是经典的分子间相互作用来重建。的;在TFIID和佐贺复合物中存在额外的组蛋白样对表明组蛋白折叠是比以前认为的更常用的介导TAF-TAF相互作用的基序。
Determination of the crystal structure of the human Tap-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 moths 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.