ATPase site architecture is required for self-assembly and remodeling activity of a hexameric AAA+ transcriptional activator.
ATPase site architecture is required for self-assembly and remodeling activity of a hexameric AAA+ transcriptional activator.
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DOI：
10.1016/j.molcel.2012.06.012
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发表时间：
2012-08-10
期刊：
影响因子：
16
通讯作者：
Buck, Martin
中科院分区：
文献类型：
--
作者：
Joly, Nicolas;Zhang, Nan;Buck, Martin
AAA+蛋白（与各种细胞活性相关的ATP酶）是利用ATP水解来重塑其底物的寡聚ATP酶。通过与GTP酶的相似性，提出ATP酶原聚体之间的核苷酸结合口袋的动态组织来调节功能。使用转录激活因子PspF作为AAA+模型，我们研究了保守残基在ATP水解和亚基间通讯中的作用。我们确定了R-指残基，并揭示了它驻留在一个保守的“R-手”基序（RxDxxxR）需要其“反式作用”的活动。此外，发散的步行者A谷氨酸残基与酪氨酸残基协同作用，在ADP依赖性亚基-亚基协调中发挥作用，形成“ADP开关”基序。另一种谷氨酸在核苷酸存在下控制六聚体的形成。总之，这些结果导致了一个“残基-核苷酸”相互作用图，AAA+核心调控的基础。步行者B和反式作用残基之间的通讯步行者A发散的谷氨酸盐的基本作用一个R-指作为R-手型谷氨酸盐的一部分AAA+蛋白中ADP的亚基-亚基协调，ADP开关
AAA+ proteins (ATPases associated with various cellular activities) are oligomeric ATPases that use ATP hydrolysis to remodel their substrates. By similarity with GTPases, a dynamic organization of the nucleotide-binding pockets between ATPase protomers is proposed to regulate functionality. Using the transcription activator PspF as an AAA+ model, we investigated contributions of conserved residues for roles in ATP hydrolysis and intersubunit communication. We determined the R-finger residue and revealed that it resides in a conserved “R-hand” motif (RxDxxxR) needed for its “trans-acting” activity. Further, a divergent Walker A glutamic acid residue acts synergistically with a tyrosine residue to function in ADP-dependent subunit-subunit coordination, forming the “ADP-switch” motif. Another glutamic acid controls hexamer formation in the presence of nucleotides. Together, these results lead to a “residue-nucleotide” interaction map upon which to base AAA+ core regulation. ► Communication between Walker B and trans-acting residues ► Essential role of the divergent Walker A glutamate ► An R-finger as part of an R-hand ► Subunit-subunit coordination by ADP in an AAA+ protein, the ADP-switch
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