Di-HAMP domains of a cytoplasmic chemoreceptor modulate nucleoid array formation and downstream signaling.

ABSTRACT: In bacterial chemosensing, environmental cues are typically sensed by bacterial transmembrane receptors known as methyl-accepting chemotaxis proteins (MCPs). MCPs form highly organized arrays using the bacterial membrane as a scaffold. These arrays amplify the signals and transduce them into a cellular response. The FrzCD cytoplasmic receptor from Myxococcus xanthus is unique due to its ability to bind DNA and use the nucleoid as a scaffold to form arrays. In this study, we identified two HAMP (histidine kinase, adenylyl cyclase, MCP, and phosphatase) domains located between the DNA binding and signaling domains of FrzCD. In vitro experiments demonstrate that the di-HAMP domain restricts FrzCD to a dimeric form in solution and modulate FrzCD affini

SUBMITTER: Jazleena PJ 

PROVIDER: S-EPMC12077210 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature