Abstract
The endosymbiosis of a free-living cyanobacterium into an ancestral eukaryote led to the evolution of the chloroplast (plastid) more than one billion years ago. Given their independent origins, plastid proliferation is restricted to the binary fission of pre-existing plastids within a cell. In the last 25 years, the structure of the supramolecular machinery regulating plastid division has been discovered, and some of its component proteins identified. More recently, isolated plastid-division machineries have been examined to elucidate their structural and mechanistic details. Furthermore, complex studies have revealed how the plastid-division machinery morphologically transforms during plastid division, and which of its component proteins play a critical role in generating the contractile force. Identifying the three-dimensional structures and putative functional domains of the component proteins has given us hints about the mechanisms driving the machinery. Surprisingly, the mechanisms driving plastid division resemble those of mitochondrial division, indicating that these division machineries likely developed from the same evolutionary origin, providing a key insight into how endosymbiotic organelles were established. These findings have opened new avenues of research into organelle proliferation mechanisms and the evolution of organelles.
Highlights
Chloroplasts produce organic molecules and oxygen via photosynthesis, directly and indirectly providing a diverse array of living organisms with the materials they need to grow and develop
It is known that plastid division is carried out by a ring-shaped supermolecule termed the plastid-division machinery, which contains three or more types of ring structures: the plastid-dividing (PD) ring, which forms the main framework of the division machinery and comprises a ring-shaped bundle of nanofilaments on the cytosolic side of the outer envelope membrane of the corresponding organelle [4,5,7]; the FtsZ ring, a single ring constructed from homologs of the bacterial fission protein FtsZ located beneath the inner envelope membrane at the division site [8]; and the dynamin ring, a disconnected ring-like structure formed of a dynamin superfamily member on the cytosolic side of the outer envelope membrane at the site of organelle division (Figure 1) [9,10]
This review summarizes and considers the domain architectures of the major proteins involved in plastid division, enabling the further exploration of the proliferation mechanisms in plastids as well as the proliferation mechanisms in mitochondria
Summary
Chloroplasts (plastids) produce organic molecules and oxygen via photosynthesis, directly and indirectly providing a diverse array of living organisms with the materials they need to grow and develop. The activity of plastids over the past billion years has resulted in the dramatic greening of the Earth. Due to their endosymbiotic origin, plastids contain their own genomes and multiply by the binary fission of pre-existing plastids [1,2,3,4]. The importance of each component for plastid division has been well studied and summarized in detail elsewhere [3,11]; the functional mechanical details of the plastid-division machinery remain unclear. It is known that the mitochondrial- and peroxisome-division machineries carry out similar division processes to those of the plastids, suggesting that the elucidation of the plastid-division system will provide insights into the proliferation of other membranous organelles within eukaryotic cells. This review summarizes and considers the domain architectures of the major proteins involved in plastid division, enabling the further exploration of the proliferation mechanisms in plastids as well as the proliferation mechanisms in mitochondria
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