NDLI: FtsZ proteins in Physcomitrella : more than just chloroplast division

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FtsZ proteins in Physcomitrella : more than just chloroplast division

Content Provider	Semantic Scholar
Author	Martin, Anja Gremillon, Louis Schween, Gabriele Reski, Ralf Sarnighausen, Eric
Copyright Year	2006
Abstract	Plastids as well as bacteria divide by binary fission. In bacteria, the division process is mediated by the action of the FtsZ (filamentous temperature sensitive Z) protein which forms a contractile ring at the future division site. Plants have acquired plastids through an endosymbiotic event. An ftsZ gene from an engulfed cyanobacterium was transferred to the host nucleus, was duplicated and equipped with sequences coding for chloroplast-targeting signals. In plants, FtsZ proteins group into two families (FtsZ1 and 2) and function in plastid division. In order to analyze the subcellular localization of FtsZ proteins in Physcomitrella patens we employed ftsZ:gfp fusions which revealed plastidic localization for FtsZ 1-1, 2-1, and 2-2 whereas FtsZ1-2 undergoes dual targeting and is found in plastids and the cytosol [1, 2]. As shown previously, the targeted knockout of ftsZ2-1 gave rise to plants with macrochloroplasts underlining the protein’s involvement in organelle division [3]. To further elucidate the individual functions of FtsZ proteins in Physcomitrella knockouts of ftsZ1-1, 1-2, and 2-2 were generated. Compared to wild type, knockout plants of ftsZ1-1 and 2-2 reveal only mild phenotypic aberrations. In contrast, loss of ftsZ1-2 leads to severe alterations in plant morphology and development. Compared to wild type, ΔftsZ1-2 lines grow slower and exhibit shorter gametophores. Chloroplast shape and size in leaflet, chloronema and caulonema cells are highly irregular. Protonema cell dimensions and leaflet cell patterning are altered as well. We therefore conclude that in Physcomitrella FtsZ1-2 is involved not only in plastid division but also plays an important role in shaping cells and chloroplasts.
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://ucjeps.berkeley.edu/bryolab/Moss2006/abstracts/Anja%20Martin.pdf
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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