Reversal of halophilicity in a protein-DNA interaction by limited mutation strategy
Reversal of halophilicity in a protein-DNA interaction by limited mutation strategy
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DOI：
10.1016/s0969-2126(02)00749-9
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发表时间：
2002-05-01
期刊：
影响因子：
5.7
通讯作者：
Ladbury, JE
中科院分区：
文献类型：
--
作者：
Bergqvist, S;Williams, MA;Ladbury, JE
对存在于不同环境中的生物体中功能同源蛋白质的基因进行比较表明，适应通常是通过现有蛋白质的突变来完成的。然而，从这样的比较，个别残留物的意义，以特定的环境适应是不是一般辨别的质量变化中发生的进化时间。这可以通过在真核生物和古细菌中发现的通用转录因子TATA结合蛋白（TBP）来举例说明。来自Pyrococcus woesei的TBP适于在高盐和高温下与DNA的最佳结合，与其最近的已知嗜温对应物相比，34%的氨基酸发生了变化。我们证明，这种蛋白质的嗜盐性可以归因于只有三个突变，揭示了嗜盐性的重要表型可以在进化过程中迅速获得。
Comparison of the genes of functionally homologous proteins in organisms existing in different environments shows that adaptation is most often accomplished by mutation of an existing protein. However, from such comparisons, the significance of individual residues to the particular environmental adaptation is not generally discernable among the mass of changes that occur over evolutionary time. This can be exemplified by the general transcription factor found in eukaryotes and archaea, the TATA binding protein (TBP). TBP from Pyrococcus woesei is adapted for optimal binding to DNA at high salt and high temperature, with 34% of the amino acids altered in comparison to its nearest known mesophilic counterpart. We demonstrate that the halophilic nature of this protein can be attributed to only three mutations, revealing that the important phenotype of halophilicity could be rapidly acquired in evolutionary time.