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Article

The plastid division protein AtMinD1 is a Ca2+-ATPase stimulated by AtMinE1.

The Journal of biological chemistry - 9 Sept 2005

Aldridge Cassie, Møller Simon Geir

Abstract excerpt

Bacteria and plastids divide symmetrically through binary fission by accurately placing the division site at midpoint, a process initiated by FtsZ polymerization, which forms a Z-ring. In Escherichia coli precise Z-ring placement at midcell depends on controlled oscillatory behavior of MinD and MinE: In the presence of ATP MinD interacts with the FtsZ inhibitor MinC and migrates to the membrane where the...

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Identifiers

PMID: 16014621
DOI: 10.1074/jbc.M505126200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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The plastid division protein AtMinD1 is a Ca2+-ATPase stimulated by AtMinE1.PMID 16014621Read ↗

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Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli.Semantic proximity Read ↗

MinE conformational dynamics regulate membrane binding, MinD interaction, and Min oscillation.Semantic proximity Read ↗

Targeted gene knockouts reveal overlapping functions of the five Physcomitrella patens FtsZ isoforms in chloroplast division, chloroplast shaping, cell patterning, plant development, and gravity sensing.Semantic proximity Read ↗

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A conserved polar region in the cell division site determinant MinD is required for responding to MinE-induced oscillation but not for localization within coiled arrays.Semantic proximity Read ↗

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