title: Further evaluation of the localization and functionality of hemagglutinin epitope- and fluorescent protein-tagged AtMinD1 in Arabidopsis thaliana.
abstract: Symmetric chloroplast division requires a prokaryote-derived division regulator protein MinD, whose subchloroplastic localization remains to be completely established. We investigated the localization and functionality of AtMinD1 (Arabidopsis thaliana MinD) fused with a dual hemagglutinin epitope (dHA) or a yellow fluorescent protein (YFP). AtMinD1-dHA, which successfully complemented the arc11/atminD1 mutant phenotype, was predominantly located at the envelope membrane and the mid-chloroplast constriction site. Meanwhile, AtMinD1-YFP was non-functional and showed suborganellar localization partly similar to that of AtMinD1-dHA. This prompts us to reevaluate earlier transgenic and transient expression studies using fluorescent protein-tagged AtMinD1.
authors: RIKEN Nishina Center, Wako, Saitama, Japan. mtf1@mac.com
authors: Makoto T
authors: MT
authors: Fujiwara
authors: Dongliang
authors: D
authors: Li
authors: Yusuke
authors: Y
authors: Kazama
authors: Tomoko
authors: T
authors: Abe
authors: Tomohide
authors: T
authors: Uno
authors: Hiroshi
authors: H
authors: Yamagata
authors: Kengo
authors: K
authors: Kanamaru
authors: Ryuuichi D
authors: RD
authors: Itoh
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D017360:Arabidopsis / Q000166:cytology / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism; D000939:Epitopes / Q000378:metabolism*; D005453:Fluorescence; D006388:Hemagglutinins / Q000378:metabolism*; D008164:Luminescent Proteins / Q000378:metabolism*; D021381:Protein Transport
chemical_list: D029681:Arabidopsis Proteins; D000939:Epitopes; D006388:Hemagglutinins; D008164:Luminescent Proteins; D000251:Adenosine Triphosphatases; C505156:MinD1 protein, Arabidopsis