Distinct functions of chloroplast FtsZ1 and FtsZ2 in Z-ring structure and remodeling.
Distinct functions of chloroplast FtsZ1 and FtsZ2 in Z-ring structure and remodeling.
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DOI:
10.1083/jcb.201205114
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发表时间:
2012-11-12
期刊:
影响因子:
--
通讯作者:
Osteryoung KW
中科院分区:
文献类型:
--
作者:
TerBush AD;Osteryoung KW
The distinct morphological and dynamic properties of their respective filaments suggest that FtsZ1 facilitates Z-ring remodeling, whereas FtsZ2 forms the Z-ring backbone during chloroplast division. FtsZ, a cytoskeletal GTPase, forms a contractile ring for cell division in bacteria and chloroplast division in plants. Whereas bacterial Z rings are composed of a single FtsZ, those in chloroplasts contain two distinct FtsZ proteins, FtsZ1 and FtsZ2, whose functional relationship is poorly understood. We expressed fluorescently tagged FtsZ1 and FtsZ2 in fission yeast to investigate their intrinsic assembly and dynamic properties. FtsZ1 and FtsZ2 formed filaments with differing morphologies when expressed separately. FRAP showed that FtsZ2 filaments were less dynamic than FtsZ1 filaments and that GTPase activity was essential for FtsZ2 filament turnover but may not be solely responsible for FtsZ1 turnover. When coexpressed, the proteins colocalized, consistent with coassembly, but exhibited an FtsZ2-like morphology. However, FtsZ1 increased FtsZ2 exchange into coassembled filaments. Our findings suggest that FtsZ2 is the primary determinant of chloroplast Z-ring structure, whereas FtsZ1 facilitates Z-ring remodeling. We also demonstrate that ARC3, a regulator of chloroplast Z-ring positioning, functions as an FtsZ1 assembly inhibitor.
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