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Nat Commun. 2019 Apr 4;10(1):1542. doi: 10.1038/s41467-019-09479-1.

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

Author information

1
Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Svante Arrhenius v. 20C, SE-10691, Stockholm, Sweden.
2
Research Group of Microbiology, Department of Bioengineering Sciences, Vrije Universiteit Brussel, Pleinlaan 2, B-1050, Brussels, Belgium.
3
Laboratory of Cell Genetics, Department of Biology, Vrije Universiteit Brussel, Pleinlaan 2, B-1050, Brussels, Belgium.
4
Molekulare Enzymtechnologie und Biochemie, Biofilm Centre, ZWU, Fakultät für Chemie, Universität Duisburg-Essen, Universitätsstr. 2, 45117, Essen, Germany.
5
Molecular Biophysics, Department of Cell and Molecular Biology, Uppsala University, Uppsala, Sweden.
6
Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Svante Arrhenius v. 20C, SE-10691, Stockholm, Sweden. Ann.Christin.Lindas@su.se.
7
Research Group of Microbiology, Department of Bioengineering Sciences, Vrije Universiteit Brussel, Pleinlaan 2, B-1050, Brussels, Belgium. Eveline.Peeters@vub.be.

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.

PMID:
30948713
PMCID:
PMC6449355
DOI:
10.1038/s41467-019-09479-1
[Indexed for MEDLINE]
Free PMC Article

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