Publikation: Differential stability of TATA box binding proteins from archaea with different optimal growth temperatures
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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 degrees C to more than 100 degrees 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(m)s) of thermal unfolding have been determined using TBPs from Methanosarcina mazei (OGT 37 degrees C) and from Methanothermobacter thermautotrophicus (OGT65 degrees C). Furthermore, the influence of protein and salt concentration on thermostability has been characterized. Together with previous studies, our results reveal that the T(m)s 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 degrees C above the OGT
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KOPITZ, Annette, Jörg SOPPA, Carsten KREJTSCHI, Karin HAUSER, 2009. Differential stability of TATA box binding proteins from archaea with different optimal growth temperatures. In: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 2009, 73(5), pp. 799-804. ISSN 1386-1425. eISSN 1873-3557. Available under: doi: 10.1016/j.saa.2009.04.002BibTex
@article{Kopitz2009-09-01Diffe-17527,
year={2009},
doi={10.1016/j.saa.2009.04.002},
title={Differential stability of TATA box binding proteins from archaea with different optimal growth temperatures},
number={5},
volume={73},
issn={1386-1425},
journal={Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy},
pages={799--804},
author={Kopitz, Annette and Soppa, Jörg and Krejtschi, Carsten and Hauser, Karin}
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<dcterms:abstract xml:lang="eng">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 degrees C to more than 100 degrees 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(m)s) of thermal unfolding have been determined using TBPs from Methanosarcina mazei (OGT 37 degrees C) and from Methanothermobacter thermautotrophicus (OGT65 degrees C). Furthermore, the influence of protein and salt concentration on thermostability has been characterized. Together with previous studies, our results reveal that the T(m)s 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 degrees C above the OGT</dcterms:abstract>
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