Lee Brian M, Xu Jing, Clarkson Bryan K, Martinez-Yamout Maria A, Dyson H Jane, Case David A, Gottesfeld Joel M, Wright Peter E
Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
J Mol Biol. 2006 Mar 17;357(1):275-91. doi: 10.1016/j.jmb.2005.12.010. Epub 2005 Dec 20.
Transcription factor IIIA (TFIIIA) is a Cys2His2 zinc finger protein that regulates expression of the 5 S ribosomal RNA gene by binding specifically to the internal control element. TFIIIA also functions in transport and storage of 5 S RNA by binding directly to the RNA transcript. To obtain insights into the mechanism by which TFIIIA recognizes 5 S RNA, we determined the solution structure of the middle three zinc fingers bound to the central core of 5 S RNA. Finger 4 utilizes "lock and key" recognition to bind in the widened major groove of the pre-structured RNA loop E motif. This interaction is mediated by direct hydrogen bonding interactions with bases. In contrast, recognition of loop A, a flexible junction of three helices, occurs by an induced fit mechanism that involves reorganization of the conserved CAUA motif and structuring of the finger 5-finger 6 interface to form a complementary RNA binding surface.
转录因子IIIA(TFIIIA)是一种Cys2His2锌指蛋白,它通过特异性结合内部控制元件来调节5S核糖体RNA基因的表达。TFIIIA还通过直接结合RNA转录本在5S RNA的运输和储存中发挥作用。为了深入了解TFIIIA识别5S RNA的机制,我们确定了与5S RNA中央核心结合的中间三个锌指的溶液结构。手指4利用“锁钥”识别方式结合在预结构化RNA环E基序变宽的大沟中。这种相互作用是由与碱基的直接氢键相互作用介导的。相比之下,环A是三个螺旋的柔性连接点,其识别是通过诱导契合机制发生的,该机制涉及保守的CAUA基序的重组以及手指5-手指6界面的结构化,以形成互补的RNA结合表面。