ArticleJournal of bacteriology2026
RodZ acts through MreBCD to activate the elongasome in
Article in Journal of bacteriology, 2026. 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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1 citing paper in PubMed.
- A broadly conserved gram-positive lipoprotein regulates cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
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7 authors.
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Abstract
Most bacteria are surrounded by a peptidoglycan (PG) matrix that maintains cell shape and provides protection against turgor pressure. In many rod-shaped bacteria, synthesis of PG along the cell cylinder is organized by the elongasome, also called the rod complex, which consists of six highly conserved proteins, including the actin-like MreB, the PG synthase complex RodA-PBP2, and three regulatory membrane proteins, MreC, MreD, and RodZ. However, how these proteins interact with each other to form the elongasome and synthesize lateral PG remains elusive. In this study, by characterizing MreC mutations affecting elongasome activity in IMPORTANCE: The elongasome, or rod complex, mediates lateral peptidoglycan (PG) synthesis during cell elongation in many rod-shaped bacteria. It consists of the cytoskeletal protein MreB, the peptidoglycan synthase RodA-PBP2, and three regulatory proteins MreCD and RodZ. Although it has been extensively studied, how its activity is controlled remains incompletely understood. Here, we reveal the roles of MreCD and RodZ in regulating elongasome activity in
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