ArticlemLife2026
Direct interaction between MreB and the RodA-PBP2 complex organizes lateral cell wall synthesis in
Article in mLife, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The elongasome, or the Rod complex, orchestrates lateral peptidoglycan (PG) synthesis in many rod-shaped bacteria. It consists of the actin-like protein MreB, the PG synthase RodA-PBP2 complex, as well as MreCD and RodZ. Although the loss or disruption of any elongasome component results in a loss of rod shape, previous studies found that a constitutively active RodA-PBP2 complex can partially bypass the requirement of MreCD and RodZ for lateral PG synthesis and restore rod shape. However, how MreB is connected to RodA-PBP2 under this situation and whether this linkage is important for elongasome activity in wild-type cells remain unknown. Here, we report the isolation of additional RodA and PBP2 variants that can partially compensate for the absence of MreCD and RodZ in lateral PG synthesis. Taking advantage of these mutants and guided by an AlphaFold 3 structural model of the elongasome complex, we discover that both the cytoplasmic region of PBP2 and the C-terminal tail of RodA interact with MreB. Moreover, disruption of these interactions results in a loss of rod shape, indicating that the interaction between MreB and RodA-PBP2 is critical for elongasome function. Taken together, our results uncover how the MreB cytoskeleton is coupled to RodA-PBP2 to organize lateral PG synthesis. These findings provide mechanistic insights into cell wall biogenesis in bacteria and offer strategies for the development of new antibiotics targeting the elongasome.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.