ArticleMolecular biology of the cell2021
Dissection of the ATPase active site of McdA reveals the sequential steps essential for carboxysome distribution.
Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 11 citations in OpenAlex.
- Unlocking the bacterial condensome: from "dark matter" to design.Molecular biology of the cell · 2026Article
- Article
- Polyphosphate acts as an architectural regulator of carbon fixation and nucleoid structure in cyanobacteria.bioRxiv : the preprint server for biology · 2026Article
- The kinetics and mobility of a ParA ATPase drive carboxysome distribution inbioRxiv : the preprint server for biology · 2026Article
- Article
- Brownian ratchet mechanisms for carboxysome positioning in bacteria.Current opinion in microbiology · 2025Review
- Organizing organelles: bacterial strategies for localizing intracellular compartments.Current opinion in microbiology · 2025Review
- Tuning the interaction of a ParA-type ATPase with its partner separates bacterial organelle positioning from partitioning.Research square · 2025Article
- Tuning the interaction of a ParA-type ATPase with its partner separates bacterial organelle positioning from partitioning.bioRxiv : the preprint server for biology · 2025Article
- An invariant C-terminal tryptophan in McdB mediates its interaction and positioning function with carboxysomes.Molecular biology of the cell · 2024Article
- Positioning of cellular components by the ParA/MinD family of ATPases.Current opinion in microbiology · 2024Review
- Dissecting the phase separation and oligomerization activities of the carboxysome positioning protein McdB.eLife · 2023Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carboxysomes, the most prevalent and well-studied anabolic bacterial microcompartment, play a central role in efficient carbon fixation by cyanobacteria and proteobacteria. In previous studies, we identified the two-component system called McdAB that spatially distributes carboxysomes across the bacterial nucleoid. Maintenance of carboxysome distribution protein A (McdA), a partition protein A (ParA)-like ATPase, forms a dynamic oscillating gradient on the nucleoid in response to the carboxysome-localized Maintenance of carboxysome distribution protein B (McdB). As McdB stimulates McdA ATPase activity, McdA is removed from the nucleoid in the vicinity of carboxysomes, propelling these proteinaceous cargos toward regions of highest McdA concentration via a Brownian-ratchet mechanism. How the ATPase cycle of McdA governs its in vivo dynamics and carboxysome positioning remains unresolved. Here, by strategically introducing amino acid substitutions in the ATP-binding region of McdA, we sequentially trap McdA at specific steps in its ATP cycle. We map out critical events in the ATPase cycle of McdA that allows the protein to bind ATP, dimerize, change its conformation into a DNA-binding state, interact with McdB-bound carboxysomes, hydrolyze ATP, and release from the nucleoid. We also find that McdA is a member of a previously unstudied subset of ParA family ATPases, harboring unique interactions with ATP and the nucleoid for trafficking their cognate intracellular cargos.
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