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J Biol Chem. 2019 May 3;294(18):7460-7471. doi: 10.1074/jbc.RA119.007709. Epub 2019 Mar 22.

Structure and interactions of the archaeal motility repression module ArnA-ArnB that modulates archaellum gene expression in Sulfolobus acidocaldarius.

Author information

1
From the Institute for Biology II, Molecular Biology of Archaea and.
2
the Philipps University, Department of Chemistry, 35032 Marburg, Germany.
3
the Spemann Graduate School of Biology and Medicine, University of Freiburg, 79104 Freiburg, Germany.
4
the ChELSI Institute, Department of Chemical and Biological Engineering, University of Sheffield, Sheffield S1 3JD, United Kingdom, and.
5
the Faculty of Science, Agriculture and Engineering, Newcastle University, Newcastle upon Tyne NE1 7RU, United Kingdom.
6
the Philipps University, Department of Chemistry, 35032 Marburg, Germany, essen@chemie.uni-marburg.de.
7
the LOEWE Center for Synthetic Microbiology, 35043 Marburg, Germany.
8
From the Institute for Biology II, Molecular Biology of Archaea and sonja.albers@biologie.uni-freiburg.de.

Abstract

Phosphorylation-dependent interactions play crucial regulatory roles in all domains of life. Forkhead-associated (FHA) and von Willebrand type A (vWA) domains are involved in several phosphorylation-dependent processes of multiprotein complex assemblies. Although well-studied in eukaryotes and bacteria, the structural and functional contexts of these domains are not yet understood in Archaea. Here, we report the structural base for such an interacting pair of FHA and vWA domain-containing proteins, ArnA and ArnB, in the thermoacidophilic archaeon Sulfolobus acidocaldarius, where they act synergistically and negatively modulate motility. The structure of the FHA domain of ArnA at 1.75 Å resolution revealed that it belongs to the subclass of FHA domains, which recognizes double-pSer/pThr motifs. We also solved the 1.5 Å resolution crystal structure of the ArnB paralog vWA2, disclosing a complex topology comprising the vWA domain, a β-sandwich fold, and a C-terminal helix bundle. We further show that ArnA binds to the C terminus of ArnB, which harbors all the phosphorylation sites identified to date and is important for the function of ArnB in archaellum regulation. We also observed that expression levels of the archaellum components in response to changes in nutrient conditions are independent of changes in ArnA and ArnB levels and that a strong interaction between ArnA and ArnB observed during growth on rich medium sequentially diminishes after nutrient limitation. In summary, our findings unravel the structural features in ArnA and ArnB important for their interaction and functional archaellum expression and reveal how nutrient conditions affect this interaction.

KEYWORDS:

Archaea; cell motility; protein phosphorylation; signal transduction; transcription regulation

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