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OsPAP10c , a novel secreted acid phosphatase in rice, plays an important role in the utilization of external organic phosphorus
Author(s) -
Lu Linghong,
Qiu Wenmin,
Gao Wenwen,
Tyerman Stephen D.,
Shou Huixia,
Wang Chuang
Publication year - 2016
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/pce.12794
Subject(s) - phosphatase , acid phosphatase , phosphate , phosphorus , rhizosphere , epidermis (zoology) , secretion , tiller (botany) , biology , biochemistry , phosphorus deficiency , organic acid , pi , rice plant , chemistry , enzyme , botany , horticulture , anatomy , genetics , organic chemistry , bacteria
Under phosphate (P i ) starvation, plants increase the secretion of purple acid phosphatases (PAPs) into the rhizosphere to scavenge organic phosphorus (P) for plant use. To date, only a few members of the PAP family have been characterized in crops. In this study, we identified a novel secreted PAP in rice, OsPAP10c , and investigated its role in the utilization of external organic P. OsPAP10c belongs to a monocotyledon‐specific subclass of Ia group PAPs and is specifically expressed in the epidermis/exodermis cell layers of roots. Both the transcript and protein levels of OsPAP10c are strongly induced by P i starvation. OsPAP10c overexpression increased acid phosphatase (APase) activity by more than 10‐fold in the culture media and almost fivefold in both roots and leaves under P i ‐sufficient and P i ‐deficient conditions. This increase in APase activity further improved the plant utilization efficiency of external organic P. Moreover, several APase isoforms corresponding to OsPAP10c were identified using in‐gel activity assays. Under field conditions with three different P i supply levels, OsPAP10c ‐overexpressing plants had significantly higher tiller numbers and shorter plant heights. This study indicates that OsPAP10c encodes a novel secreted APase that plays an important role in the utilization of external organic P in rice.