Footprints of aminoacyl-tRNA synthetases are everywhere
Footprints of aminoacyl-tRNA synthetases are everywhere
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DOI:
10.1016/s0968-0004(00)01553-x
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发表时间:
2000-05-01
影响因子:
13.8
通讯作者:
De Pouplana, LR
中科院分区:
文献类型:
--
作者:
Schimmel, P;De Pouplana, LR
Figure 1 Model for the emergence of aminoacyl-tRNA synthetase (aaRS)-like proteins from extant aaRS structures or their modular precursors. The class-defining domain of extant aminoacyl-tRNA synthetases (in gray) is likely to be the oldest module and interacted with a minihelix-like domain (exemplified by a minihelix structure) through RNA-binding elements that were added (dashed lines)(see Ref. 9). Additional domains and insertions in extant aaRSs (in red and blue) were added later, perhaps to increase the specificity of each enzyme for its cognate tRNAs through new molecular interactions13. This process (depicted by dashed arrows) gave rise to the extant forms of aminoacyl-tRNA synthetases. At any stage of this evolutionary process, single domains, or combinations of them, can have diverged (solid arrows) to generate the extant aaARS-like proteins, represented in the box to the right of the figure.