Transmembrane signaling and cytoplasmic signal conversion by dimeric transmembrane helix 2 and a linker domain of the DcuS sensor kinase.

ABSTRACT: Transmembrane (TM) signaling is a key process of membrane-bound sensor kinases. The C₄-dicarboxylate (fumarate) responsive sensor kinase DcuS of Escherichia coli is anchored by TM helices TM1 and TM2 in the membrane. Signal transmission across the membrane relies on the piston-type movement of the periplasmic part of TM2. To define the role of TM2 in TM signaling, we use oxidative Cys cross-linking to demonstrate that TM2 extends over the full distance of the membrane and forms a stable TM homodimer in both the inactive and fumarate-activated state of DcuS. An S₁₈₆xxxGxxxG₁₉₄ motif is required for the stability and function of the TM2 homodimer. The TM2 helix further extends on the periplasmic side into the α6-helix of the sensory PASP domain and on the cyt

SUBMITTER: Stopp M 

PROVIDER: S-EPMC7857512 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature