Further evaluation of the localization and functionality of hemagglutinin epitope- and fluorescent protein-tagged AtMinD1 in Arabidopsis thaliana.
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.
Fujiwara
Makoto T
MT
RIKEN Nishina Center, Wako, Saitama, Japan. mtf1@mac.com
Li
Dongliang
D
Kazama
Yusuke
Y
Abe
Tomoko
T
Uno
Tomohide
T
Yamagata
Hiroshi
H
Kanamaru
Kengo
K
Itoh
Ryuuichi D
RD
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
D029681:Arabidopsis Proteins; D000939:Epitopes; D006388:Hemagglutinins; D008164:Luminescent Proteins; D000251:Adenosine Triphosphatases; C505156:MinD1 protein, Arabidopsis