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

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/p

SUBMITTER: Hoffmann L 

PROVIDER: S-EPMC6509490 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature