Burrows Patricia C
Department of Biological Sciences, Sir Alexander Fleming Building Imperial College London, South Kensington Campus, London SW7 2AZ.
Bioessays. 2003 Dec;25(12):1150-3. doi: 10.1002/bies.10388.
Transcription initiation by sigma(54)-RNA polymerase (RNAP) relies explicitly on a transient interaction with a complex molecular machine belonging to the AAA+ (ATPases associated with various cellular activities) superfamily. Members of the AAA+ superfamily convert chemical energy derived from NTP hydrolysis to a mechanical force used to remodel their target substrate. Recently Bordes and colleagues,1 using a protein fragmentation approach, identified a unique sequence within sigma(54)-dependent transcriptional activators that constitutes a sigma(54)-binding interface. This interface is not static, but subject to nucleotide-dependent movement which may represent a common mechanism for controlling output that has been adopted by other AAA+ proteins.
由σ⁵⁴-RNA聚合酶（RNAP）引发的转录起始明确依赖于与属于AAA⁺（与各种细胞活动相关的ATP酶）超家族的复杂分子机器的短暂相互作用。AAA⁺超家族的成员将NTP水解产生的化学能转化为用于重塑其靶底物的机械力。最近，博尔德斯及其同事1采用蛋白质片段化方法，在依赖σ⁵⁴的转录激活因子中鉴定出一个独特序列，该序列构成了σ⁵⁴结合界面。这个界面不是静态的，而是会发生依赖核苷酸的移动，这可能代表了一种已被其他AAA⁺蛋白采用的控制输出的常见机制。
