Translation termination in pyrrolysine-utilizing archaea.

Translation termination in pyrrolysine-utilizing archaea.
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DOI:
10.1016/j.febslet.2009.09.044
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发表时间:
2009-11-03
期刊:
影响因子:
3.5
通讯作者:
Kisselev L
Kisselev L
中科院分区:
生物学3区
文献类型:
--
作者:
Alkalaeva E;Eliseev B;Ambrogelly A;Vlasov P;Kondrashov FA;Gundllapalli S;Frolova L;Söll D;Kisselev L

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虽然一些数据将古细菌和真核生物的翻译联系起来,但古细菌中蛋白质合成的整体机制仍然很模糊。古细菌(aRF 1)和真核生物(eRF 1)的单释放因子识别所有三个终止密码子。古菌属甲烷菌科含有两个aRF 1同源物,并且还使用UAG终止来编码第22个氨基酸吡咯赖氨酸。在这里,我们提供了一个分析的最后阶段的古细菌翻译利用吡咯赖氨酸的物种。我们证明,只有一个两个甲烷八叠球菌barkeri aRF1同源物具有活性,并承认所有三个终止密码子。第二个aRF1同源物可能具有另一个未知功能。本文还讨论了甲藻科植物中吡咯赖氨酸掺入的机制。
Although some data link archaeal and eukaryotic translation, the overall mechanism of protein synthesis in archaea remains largely obscure. Both archaeal (aRF1) and eukaryotic (eRF1) single release factors recognize all three stop codons. The archaeal genus Methanosarcinaceae contains two aRF1 homologs, and also uses the UAG stop to encode the 22nd amino acid, pyrrolysine. Here we provide an analysis of the last stage of archaeal translation in pyrrolysine-utilizing species. We demonstrated that only one of two Methanosarcina barkeri aRF1 homologs possesses activity and recognizes all three stop codons. The second aRF1 homolog may have another unknown function. The mechanism of pyrrolysine incorporation in the Methanosarcinaceae is discussed.
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