English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance Expression of bacterial genes in response to various cues is predominantly regulated by 2- or multicomponent systems with autophosphorylation of a histidine kinase (HK), the first component, being controlled by an N-terminal sensor domain. This is followed by phosphotransfer to the receiver domain (Rec) of a cognate transcription factor. In about 20% of all cases, HK core and Rec are fused to form a hybrid HK (HHK). Here, we show the first full-length structure of an HHK and reveal how it gets activated by the second-messenger c-di-GMP that binds to a dedicated pseudo-Rec domain. The mechanism is fundamentally distinct from the canonical mechanism of HK regulation, but may be operational in many HHKs with a predicted pseudo-Rec domain.

Hybrid histidine kinase activation by cyclic di-GMP–mediated domain liberation