Context-dependent anticodon recognition by class I lysyl-tRNA synthetases.
Context-dependent anticodon recognition by class I lysyl-tRNA synthetases.
复制标题
I 类赖氨酰-tRNA 合成酶的上下文依赖性反密码子识别。
DOI:
10.1073/pnas.97.26.14224
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发表时间:
2000
影响因子:
11.1
通讯作者:
Ibba,M
中科院分区:
文献类型:
--
作者:
Söll,D;Becker,HD;Plateau,P;Blanquet,S;Ibba,M
Lysyl-tRNA synthesis is catalyzed by two unrelated families of aminoacyl-tRNA synthetases. In most bacteria and all eukarya, the known lysyl-tRNA synthetases (LysRSs) are subclass IIb-type aminoacyl-tRNA synthetases, whereas many archaea and a scattering of bacteria contain an unrelated class I-type LysRS. Examination of the recognition of partially modified tRNALysanticodon variants by a bacterial (fromBorrelia burgdorferi) and an archaeal (fromMethanococcus maripaludis) class I lysyl-tRNA synthetase revealed differences in the pattern of anticodon recognition between the two enzymes. U35 and U36 were both important for recognition by theB. burgdorferienzyme, whereas only U36 played a role in recognition byM. maripaludisLysRS. Examination of the phylogenetic distribution of class I LysRSs suggested a correlation between recognition of U35 and U36 and the presence of asparaginyl-tRNA synthetase (AsnRS), which also recognizes U35 and U36 in the anticodon of tRNAAsn. However, the class II LysRS ofHelicobacter pylori, an organism that lacks AsnRS, also recognizes both U35 and U36, indicating that the presence of AsnRS has solely influenced the phylogenetic distribution of class I LysRSs. These data suggest that competition between unrelated aminoacyl-tRNA synthetases for overlapping anticodon sequences is a determinant of the phylogenetic distribution of extant synthetase families. Such patterns of competition also provide a basis for the two separate horizontal gene transfer events hypothesized in the evolution of the class I lysyl-tRNA synthetases.