Details

Autor(en) / Beteiligte

• Luo, Jiajia
• Chen, Zhijian
• Huang, Rui
• Wu, Yuanhang
• Liu, Chun
• Cai, Zeping
• Dong, Rongshu
• Arango, Jacobo
• Rao, Idupulapati Madhusudana
• Schultze‐Kraft, Rainer
• Liu, Guodao
• Liu, Pandao

Titel

Multi‐omics analysis reveals the roles of purple acid phosphatases in organic phosphorus utilization by the tropical legume Stylosanthes guianensis

Ist Teil von

• The Plant journal : for cell and molecular biology, 2024-02, Vol.117 (3), p.729-746

Ort / Verlag

England: Blackwell Publishing Ltd

Erscheinungsjahr

2024

Quelle

Wiley Online Library All Journals

Beschreibungen/Notizen

• SUMMARY Stylo (Stylosanthes guianensis) is a tropical legume known for its exceptional tolerance to low phosphate (Pi), a trait believed to be linked to its high acid phosphatase (APase) activity. Previous studies have observed genotypic variations in APase activity in stylo; however, the gene encoding the crucial APase responsible for this variation remains unidentified. In this study, transcriptomic and proteomic analyses were employed to identify eight Pi starvation‐inducible (PSI) APases belonging to the purple APase (PAP) family in the roots of stylo and seven in the leaves. Among these PSI‐PAPs, SgPAP7 exhibited a significantly positive correlation in its expression levels with the activities of both internal APase and root‐associated APase across 20 stylo genotypes under low‐Pi conditions. Furthermore, the recombinant SgPAP7 displayed high catalytic activity toward adenosine 5′‐diphosphate (ADP) and phosphoenolpyruvate (PEP) in vitro. Overexpression (OE) of SgPAP7 in Arabidopsis facilitated exogenous organic phosphorus utilization. Moreover, SgPAP7 OE lines showed lower shoot ADP and PEP levels than the wild type, implying that SgPAP7 is involved in the catabolism and recycling of endogenous ADP and PEP, which could be beneficial for plant growth in low‐Pi soils. In conclusion, SgPAP7 is a key gene with a major role in stylo adaptation to low‐Pi conditions by facilitating the utilization of both exogenous and endogenous organic phosphorus sources. It may also function as a PEP phosphatase involved in a glycolytic bypass pathway that minimizes the need for adenylates and Pi. Thus, SgPAP7 could be a promising target for improving tolerance of crops to low‐Pi availability. Significance Statement Identifying key genes responsible for genotypic variations in acid phosphatase (APase) activity is of significant importance for deciphering the low phosphate (Pi) tolerance traits in stylo. This study characterizes a key APase, SgPAP7, which facilitates stylo adaptation to low‐Pi availability by simultaneously performing the dual functions of internal APase and root‐associated APase, participating in the scavenging and recycling of Pi from organic phosphorus sources, including ADP and PEP.