Goodrich J A, Tjian R
Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Curr Opin Cell Biol. 1994 Jun;6(3):403-9. doi: 10.1016/0955-0674(94)90033-7.
Recent evidence indicates that the TATA-binding protein (TBP) is central to transcription by all three eukaryotic RNA polymerases (I, II, and III). Interestingly, the majority of the TBP does not appear to be free protein in vivo. Instead, it is found associated with other factors (TAFs) in multisubunit complexes. The past year has brought significant advances in our understanding of the subunit compositions and biochemical functions of these complexes. In addition, the crystal structures of the TBP core domain and the TBP-TATA box DNA complex provide new insights into how this small protein might interact with many different partners.
最近的证据表明，TATA结合蛋白（TBP）对于所有三种真核生物RNA聚合酶（I、II和III）的转录至关重要。有趣的是，大多数TBP在体内似乎并非游离蛋白。相反，它存在于多亚基复合物中，并与其他因子（TAFs）相关联。过去一年里，我们对这些复合物的亚基组成和生化功能的理解取得了重大进展。此外，TBP核心结构域和TBP-TATA盒DNA复合物的晶体结构为这种小蛋白如何与许多不同的伙伴相互作用提供了新的见解。
