TY - JOUR
T1 - Identification and characterization of an Arabidopsis phosphate starvation-induced secreted acid phosphatase as a vegetative storage protein
AU - Sun, Lichao
AU - Wang, Liangsheng
AU - Zheng, Zai
AU - Liu, Dong
N1 - Publisher Copyright:
© 2018 Elsevier B.V.
PY - 2018/12
Y1 - 2018/12
N2 - Induction and secretion of acid phosphatases is an adaptive response of plants to phosphate starvation. The secreted acid phosphatases are believed to scavenge phosphate from organophosphate compounds in the rhizosphere, thereby increasing phosphate availability for plant absorption. To date, however, all of the characterized phosphate starvation-induced secreted acid phosphatases in plants belong to a unique acid phosphatases subfamily, called purple acid phosphatase. In this work, we identified a phosphate starvation-induced secreted acid phosphatase in Arabidopsis as a vegetative storage protein, AtVSP3. AtVSP3 exists as a monomer with molecular weight of 29 kDa. The activity of recombinant AtVSP3 protein is activated by Mg2+, Co2+, and Ca2+. AtVSP3 has an optimal pH of 6.5 for its APase activity and is relatively thermostable. The transcription of AtVSP3 is induced in roots by phosphate starvation, and the accumulation of AtVSP3 protein is high in roots and siliques. Additional research is needed to determine the function of AtVSP3 in plant responses to stress conditions.
AB - Induction and secretion of acid phosphatases is an adaptive response of plants to phosphate starvation. The secreted acid phosphatases are believed to scavenge phosphate from organophosphate compounds in the rhizosphere, thereby increasing phosphate availability for plant absorption. To date, however, all of the characterized phosphate starvation-induced secreted acid phosphatases in plants belong to a unique acid phosphatases subfamily, called purple acid phosphatase. In this work, we identified a phosphate starvation-induced secreted acid phosphatase in Arabidopsis as a vegetative storage protein, AtVSP3. AtVSP3 exists as a monomer with molecular weight of 29 kDa. The activity of recombinant AtVSP3 protein is activated by Mg2+, Co2+, and Ca2+. AtVSP3 has an optimal pH of 6.5 for its APase activity and is relatively thermostable. The transcription of AtVSP3 is induced in roots by phosphate starvation, and the accumulation of AtVSP3 protein is high in roots and siliques. Additional research is needed to determine the function of AtVSP3 in plant responses to stress conditions.
KW - Biochemical characterization
KW - Expression patterns
KW - Phosphate starvation
KW - Secreted acid phosphatase
KW - Vegetative storage protein
UR - http://www.scopus.com/inward/record.url?scp=85054169748&partnerID=8YFLogxK
U2 - 10.1016/j.plantsci.2018.09.016
DO - 10.1016/j.plantsci.2018.09.016
M3 - Article
C2 - 30466593
AN - SCOPUS:85054169748
SN - 0168-9452
VL - 277
SP - 278
EP - 284
JO - Plant Science
JF - Plant Science
ER -