caa a22 4500 445818352 CHVBK 20180317145235.0 cr unu---uuuuu 170323e20111101xx s 000 0 eng 10.1007/s00792-011-0395-y doi (NATIONALLICENCE)springer-10.1007/s00792-011-0395-y Archaeal transcriptional regulation of the prokaryotic KdpFABC complex mediating K+ uptake in H. salinarum [Elektronische Daten] [Dorthe Kixmüller, Henrik Strahl, Andy Wende, Jörg-Christian Greie] The genome of the halophilic archaeon Halobacterium salinarum encodes the high-affinity ATP-dependent K+ uptake system Kdp. Previous studies have shown that the genes coding for the KdpFABC complex are arranged in a kdpFABCQ gene cluster together with an additional gene kdpQ. In bacteria, expression of the kdpFABC genes is generally regulated by the dedicated sensor kinase/response regulator pair KdpD/KdpE, which are absent in H. salinarum. Surprisingly, H. salinarum expresses the kdp genes in a manner which is strikingly similar to Escherichia coli. In this study, we show that the halobacterial kdpFABCQ genes constitute an operon and that kdpFABCQ expression is subject to a complex regulatory mechanism involving a negative transcriptional regulator and is further modulated via a so far unknown mechanism. We describe how the regulation of kdp gene expression is facilitated in H. salinarum in contrast to its bacterial counterparts. Whereas the Kdp system fulfils the same core function as an ATP-driven K+ uptake system in both archaea and bacteria, the different mechanisms involved in the regulation of gene expression appear to have evolved separately, possibly reflecting a different physiological role of ATP-driven K+ uptake in halophilic archaea. Springer, 2011 Haloarchaea nationallicence Halobacterium nationallicence Potassium uptake nationallicence KdpFABC nationallicence KdpQ nationallicence KdpD nationallicence Gene regulation nationallicence TFB : Transcription factor B nationallicence BRE : Transcription factor B recognition element nationallicence TBP : TATA-box binding protein nationallicence INR : Transcription initiation region nationallicence Usp : Universal stress protein nationallicence RT : Reverse transcriptase nationallicence Kixmüller Dorthe Fachbereich Biologie/Chemie, Universität Osnabrück, Barbarastraße 11, 49076, Osnabrück, Germany aut Strahl Henrik Newcastle University, Centre for Bacterial Cell Biology, Richardson Road, NE2 4AX, Newcastle upon Tyne, UK aut Wende Andy QIAGEN GmbH, Qiagen-Str. 1, 40724, Hilden, Germany aut Greie Jörg-Christian Fachbereich Biologie/Chemie, Universität Osnabrück, Barbarastraße 11, 49076, Osnabrück, Germany aut Extremophiles Springer Japan 15/6(2011-11-01), 643-652 1431-0651 15:6<643 2011 15 792 https://doi.org/10.1007/s00792-011-0395-y text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00792-011-0395-y text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kixmüller Dorthe Fachbereich Biologie/Chemie, Universität Osnabrück, Barbarastraße 11, 49076, Osnabrück, Germany aut NATIONALLICENCE 700 1- Strahl Henrik Newcastle University, Centre for Bacterial Cell Biology, Richardson Road, NE2 4AX, Newcastle upon Tyne, UK aut NATIONALLICENCE 700 1- Wende Andy QIAGEN GmbH, Qiagen-Str. 1, 40724, Hilden, Germany aut NATIONALLICENCE 700 1- Greie Jörg-Christian Fachbereich Biologie/Chemie, Universität Osnabrück, Barbarastraße 11, 49076, Osnabrück, Germany aut NATIONALLICENCE 773 0- Extremophiles Springer Japan 15/6(2011-11-01), 643-652 1431-0651 15:6<643 2011 15 792 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer