ArticleThe Journal of biological chemistry2025
Structural and biophysical insights into RomR, MglB, and MglC interactions involved in regulating cell polarity in Myxococcus xanthus.
Article in The Journal of biological chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- The polar landscape of bacterial pathogens and predators.Current opinion in microbiology · 2026Review
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3 authors.
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Abstract
Cell polarity is an important phenomenon that helps in modulating many essential cellular functions, including motility in bacteria. In Myxococcus xanthus, cell polarity is mediated by a complex network of interacting proteins, including Ras-like GTPase protein Mgl (mutual gliding-motility protein) A, MglB, MglC, and RomRX (required for motility response regulator) complex. The interaction dynamics of these proteins are essential for the localization and switching of interacting partners. In this study, we performed a detailed interaction analysis to determine binding affinities and stoichiometry of the complexes involved in polarity reversal. We show that the RomR C-terminal helix, RomR
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