AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes.
AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes.
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DOI：
10.1101/gr.9.1.27
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发表时间：
1999-01
期刊：
影响因子：
7
通讯作者：
A. F. Neuwald;L. Aravind;J. Spouge;E. Koonin
中科院分区：
文献类型：
--
作者：
A. F. Neuwald;L. Aravind;J. Spouge;E. Koonin
使用迭代数据库搜索和多序列比对的计算机方法的组合，我们表明，AAA家族的ATP酶相关的蛋白质序列远比以前报道的更为普遍。其中包括Lon和Clp蛋白酶的调节组分，这些蛋白质参与DNA复制、重组和限制（包括起始识别复合物的亚基、复制因子C蛋白、MCM DNA许可因子和细菌DnaA、RuvB和McrB蛋白）、原核NtrC相关转录调节因子、芽孢杆菌孢子形成蛋白SpoVJ、Mg 2+和Co 2+螯合酶，盐杆菌GvpN气泡合成蛋白、动力蛋白马达蛋白、扭转蛋白A和Rubisco活化酶。根据大肠杆菌DNA聚合酶III的夹加载子δ '亚基和N-乙基马来酰亚胺敏感性融合蛋白的六聚化组分的结构，这些序列的比对提供了对这些蛋白质的结构和机制的见解，这些蛋白质被统称为AAA+类。全基因组分析表明，这类是古老的，并已经历了相当大的功能分歧之前出现的主要部门的生活。这些蛋白质通常执行伴侣样功能，帮助蛋白质复合物的组装、操作或分解。通常与这类相关的六聚体结构可以提供DNA或RNA可以穿过的孔;这对于DNA-蛋白质复合物的组装或重塑可能是重要的。
Using a combination of computer methods for iterative database searches and multiple sequence alignment, we show that protein sequences related to the AAA family of ATPases are far more prevalent than reported previously. Among these are regulatory components of Lon and Clp proteases, proteins involved in DNA replication, recombination, and restriction (including subunits of the origin recognition complex, replication factor C proteins, MCM DNA-licensing factors and the bacterial DnaA, RuvB, and McrB proteins), prokaryotic NtrC-related transcription regulators, the Bacillus sporulation protein SpoVJ, Mg2+, and Co2+ chelatases, the Halobacterium GvpN gas vesicle synthesis protein, dynein motor proteins, TorsinA, and Rubisco activase. Alignment of these sequences, in light of the structures of the clamp loader delta' subunit of Escherichia coli DNA polymerase III and the hexamerization component of N-ethylmaleimide-sensitive fusion protein, provides structural and mechanistic insights into these proteins, collectively designated the AAA+ class. Whole-genome analysis indicates that this class is ancient and has undergone considerable functional divergence prior to the emergence of the major divisions of life. These proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes. The hexameric architecture often associated with this class can provide a hole through which DNA or RNA can be thread; this may be important for assembly or remodeling of DNA-protein complexes.