Differential stability of TATA box binding proteins from archaea with different optimal growth temperatures

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• 作者：Annette Kopitz ; J&#xf6 ; rg Soppa ; Carsten Krejtschi ; Karin Hauser
• 关键词：TATA box binding protein ; Archaea ; Thermoadaptation ; Protein stability ; Infrared spectroscopy
• 刊名：Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
• 出版年：2009
• 出版时间：1 September 2009
• 年：2009
• 卷：73
• 期：5
• 页码：799-804
• 全文大小：462 K

文摘

The TATA box binding protein (TBP) is involved in promoter recognition, the first step of transcription initiation. TBP is universally conserved and essential in archaea and eukaryotes. In archaea, TBPs have to be stable and to function in species that cover an extremely wide range of optimal growth temperatures (OGTs), from below 0 °C to more than 100 °C. Thus, the archaeal TBP family is ideally suited to study the evolutionary adaptation of proteins to an extremely wide range of temperatures. We characterized the thermostability of one mesophilic and one thermophilic TBP by infrared spectroscopy. Transition temperatures (T_ms) of thermal unfolding have been determined using TBPs from Methanosarcina mazei (OGT 37 °C) and from Methanothermobacter thermautotrophicus (OGT 65 °C). Furthermore, the influence of protein and salt concentration on thermostability has been characterized. Together with previous studies, our results reveal that the T_ms of archaeal TBPs are closely correlated with the OGTs of the respective species. Noteworthy, this is also true for the TBP from M. mazei representing the first characterized TBP from a mesophilic archaeon. In contrast, the only characterized eukaryotic TBP of the mesophilic plant Arabidopsis thaliana has a T_m more than 40 °C above the OGT.