ArticleProceedings of the National Academy of Sciences of the United States of America2005
The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 130 citations in OpenAlex.
- Twin-arginine transport complex plays an essential role inMolecular biology of the cell · 2026Article
- Twin-arginine transport complex plays an essential role inbioRxiv : the preprint server for biology · 2025Article
- The two-component system ChvGI maintains cell envelope homeostasis in Caulobacter crescentus.PLoS genetics · 2022Article
- The crystal structure of MreC provides insights into polymer formation.FEBS open bio · 2022Article
- Identification of potential regulatory domains within the MreC and MreD components of the cell elongation machinery.Journal of bacteriology · 2021Article
- Disruption of the MreB Elongasome Is Overcome by Mutations in the Tricarboxylic Acid Cycle.Frontiers in microbiology · 2021Article
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- Membrane molecular crowding enhances MreB polymerization to shape synthetic cells from spheres to rods.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A specialized MreB-dependent cell wall biosynthetic complex mediates the formation of stalk-specific peptidoglycan in Caulobacter crescentus.PLoS genetics · 2019Article
- Association between cell growth and vancomycin resistance in clinical community-associated methicillin-resistantInfection and drug resistance · 2019Article
- Molecular architecture of the PBP2-MreC core bacterial cell wall synthesis complex.Nature communications · 2017Article
- Shapeshifting to Survive: Shape Determination and Regulation in Caulobacter crescentus.Trends in microbiology · 2017Review
- Coarse-grained simulations of bacterial cell wall growth reveal that local coordination alone can be sufficient to maintain rod shape.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Bacterial morphogenesis and the enigmatic MreB helix.Nature reviews. Microbiology · 2015Article
- The Rho Termination Factor of Clostridium botulinum Contains a Prion-Like Domain with a Highly Amyloidogenic Core.Frontiers in microbiology · 2015Article
- Article
- Reconstruction of mreB expression in Staphylococcus aureus via a collection of new integrative plasmids.Applied and environmental microbiology · 2014Article
- Exploring bacterial cell biology with single-molecule tracking and super-resolution imaging.Nature reviews. Microbiology · 2014Review
- Motion of variable-length MreB filaments at the bacterial cell membrane influences cell morphology.Molecular biology of the cell · 2013Article
- Direct interaction of FtsZ and MreB is required for septum synthesis and cell division in Escherichia coli.The EMBO journal · 2013Article
2 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial actin homolog, MreB, forms helical cables within the cell that are required for maintenance of a rod shape. These helical structures are thought to be involved in the spatial organization of cell wall (peptidoglycan) synthesizing complexes of penicillin-binding proteins (PBPs). Here, we examined the role of the MreC cell shape protein in this process in Caulobacter crescentus. Subcellular fractionation experiments showed that MreC is a periplasmic protein and, as assayed by immunofluorescence microscopy, adopted helical or banded patterns along the cell length reminiscent of those formed by MreB and PBP2. The pattern of MreC and PBP2 localization remained when MreB cables were disrupted by treatment with the inhibitor A22. However, long-term absence of MreB led to cell shape changes and an eventual loss of MreC localization, suggesting that an independent structure, perhaps an intact peptidoglycan layer, contributes to the MreC localization pattern. Using affinity chromatography with MreC covalently bound to Sepharose, we isolated several PBPs from cell extracts that eluted from the column as heterogeneous complexes. In this same experiment, using mass spectrometry-based protein identification, we identified several outer membrane proteins, including TonB-dependent receptor transport proteins, that interacted with MreC. Imaging live cells containing fusions of these outer membrane proteins to green fluorescent protein showed that they adopted a subcellular localization pattern that was similar to that of MreC. These results suggest that MreC may function in the spatial organization of PBPs as well as other proteins that lie outside the cytoplasmic membrane.
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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.