title: Interdependency of formation and localisation of the Min complex controls symmetric plastid division.
abstract: Plastid division represents a fundamental biological process essential for plant development; however, the molecular basis of symmetric plastid division is unclear. AtMinE1 plays a pivotal role in selection of the plastid division site in concert with AtMinD1. AtMinE1 localises to discrete foci in chloroplasts and interacts with AtMinD1, which shows a similar localisation pattern. Here, we investigate the importance of Min protein complex formation during the chloroplast division process. Dissection of the assembly of the Min protein complex and determination of the interdependency of complex assembly and localisation in planta allow us to present a model of the molecular basis of selection of the division site in plastids. Moreover, functional analysis of AtMinE1 in bacteria demonstrates the level of functional conservation and divergence of the plastidic MinE proteins.
authors.affiliation: Centre for Organelle Research, Department of Mathematics and Natural Sciences, University of Stavanger, 4036 Stavanger, Norway.
authors.forename: Jodi
authors.initials: J
authors.lastname: Maple
authors.forename: Simon G
authors.initials: SG
authors.lastname: Møller
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D017360:Arabidopsis / Q000166:cytology / Q000502:physiology; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000378:metabolism; D018087:Plastids / Q000502:physiology* / Q000648:ultrastructure; D016415:Sequence Alignment; D020798:Two-Hybrid System Techniques
chemical_list: D029681:Arabidopsis Proteins; D018797:Cell Cycle Proteins; C465003:MinE1 protein, Arabidopsis; D046912:Multiprotein Complexes