A TetR-family transcription factor regulates fatty acid metabolism in the archaeal model organism Sulfolobus acidocaldarius

Kun Wang, David Sybers, Hassan Ramadan Maklad, Liesbeth Lemmens, Charlotte Lewyllie, Xiaoxiao Zhou, Frank Schult, Christopher Bräsen, Bettina Siebers, Karin Valegård, Ann-Christin Lindås () and Eveline Peeters ()
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Kun Wang: The Wenner-Gren Institute, Stockholm University
David Sybers: Vrije Universiteit Brussel
Hassan Ramadan Maklad: Vrije Universiteit Brussel
Liesbeth Lemmens: Vrije Universiteit Brussel
Charlotte Lewyllie: Vrije Universiteit Brussel
Xiaoxiao Zhou: Biofilm Centre, ZWU, Fakultät für Chemie, Universität Duisburg-Essen
Frank Schult: Biofilm Centre, ZWU, Fakultät für Chemie, Universität Duisburg-Essen
Christopher Bräsen: Biofilm Centre, ZWU, Fakultät für Chemie, Universität Duisburg-Essen
Bettina Siebers: Biofilm Centre, ZWU, Fakultät für Chemie, Universität Duisburg-Essen
Karin Valegård: Uppsala University
Ann-Christin Lindås: The Wenner-Gren Institute, Stockholm University
Eveline Peeters: Vrije Universiteit Brussel

Nature Communications, 2019, vol. 10, issue 1, 1-16

Abstract: Abstract Fatty acid metabolism and its regulation are known to play important roles in bacteria and eukaryotes. By contrast, although certain archaea appear to metabolize fatty acids, the regulation of the underlying pathways in these organisms remains unclear. Here, we show that a TetR-family transcriptional regulator (FadRSa) is involved in regulation of fatty acid metabolism in the crenarchaeon Sulfolobus acidocaldarius. Functional and structural analyses show that FadRSa binds to DNA at semi-palindromic recognition sites in two distinct stoichiometric binding modes depending on the operator sequence. Genome-wide transcriptomic and chromatin immunoprecipitation analyses demonstrate that the protein binds to only four genomic sites, acting as a repressor of a 30-kb gene cluster comprising 23 open reading frames encoding lipases and β-oxidation enzymes. Fatty acyl-CoA molecules cause dissociation of FadRSa binding by inducing conformational changes in the protein. Our results indicate that, despite its similarity in overall structure to bacterial TetR-family FadR regulators, FadRSa displays a different acyl-CoA binding mode and a distinct regulatory mechanism.

Date: 2019
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DOI: 10.1038/s41467-019-09479-1

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