Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from three kingdoms.

Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from three kingdoms.
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DOI:
10.1093/nar/gkm417
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发表时间:
2007
影响因子:
14.9
通讯作者:
Nakamura KT
Nakamura KT
中科院分区:
生物学2区
文献类型:
--
作者:
Tsunoda M;Kusakabe Y;Tanaka N;Ohno S;Nakamura M;Senda T;Moriguchi T;Asai N;Sekine M;Yokogawa T;Nishikawa K;Nakamura KT

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酪氨酰-tRNA合成酶(tyrosyl-tRNA synthetase,TyrRSs)对tRNA的特异性氨酰化依赖于同源tRNatyr中的同源性决定因素。我们测定了酿酒酵母TyrRS(SceTyrRS)与Tyr-AMP类似物和天然tRNatyr(GΨA)的络合物的晶体结构。TyrRS-tRNatyr复合体的结构信息现在是三个王国的全线信息。由于古生菌/真核生物TyrRSs-tRNatyr对与细菌对不发生交叉反应,古生菌/真核TyrRSs对身份决定簇的识别模式可能彼此相似,但与细菌TyrRSs的识别模式不同。然而,有趣的是,SceTyrRS和古生菌TyrRS的tRNatyr识别模式既有相似之处,也有不同之处:SceTyrRS对C1-G72碱基对的识别与古生菌TyrRS相似,而SceTyrRS对A73的识别不同于古生菌TyrRS,但与细菌TyrRS相似。因此,古生物/真核生物和细菌TyrRS-tRNatyr之间缺乏交叉反应很可能是由于tRNatyr的受体茎的最后一个碱基对的不同序列(C1-G72对G1-C72)。另一方面,Tyr-AMP的识别模式在三国的TyrRS中是保守的。
The specific aminoacylation of tRNA by tyrosyl-tRNA synthetases (TyrRSs) relies on the identity determinants in the cognate tRNATyrs. We have determined the crystal structure of Saccharomyces cerevisiae TyrRS (SceTyrRS) complexed with a Tyr-AMP analog and the native tRNATyr(GΨA). Structural information for TyrRS–tRNATyr complexes is now full-line for three kingdoms. Because the archaeal/eukaryotic TyrRSs–tRNATyrs pairs do not cross-react with their bacterial counterparts, the recognition modes of the identity determinants by the archaeal/eukaryotic TyrRSs were expected to be similar to each other but different from that by the bacterial TyrRSs. Interestingly, however, the tRNATyr recognition modes of SceTyrRS have both similarities and differences compared with those in the archaeal TyrRS: the recognition of the C1-G72 base pair by SceTyrRS is similar to that by the archaeal TyrRS, whereas the recognition of the A73 by SceTyrRS is different from that by the archaeal TyrRS but similar to that by the bacterial TyrRS. Thus, the lack of cross-reactivity between archaeal/eukaryotic and bacterial TyrRS-tRNATyr pairs most probably lies in the different sequence of the last base pair of the acceptor stem (C1-G72 vs G1-C72) of tRNATyr. On the other hand, the recognition mode of Tyr-AMP is conserved among the TyrRSs from the three kingdoms.
DOI: 10.1016/s0300-9084(99)80057-1
发表时间: 1999-03-01
期刊: BIOCHIMIE
影响因子: 3.9
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发表时间: 2006
影响因子: 14.9
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期刊: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
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期刊: FEBS LETTERS
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