OsPAP26 Encodes a Major Purple Acid Phosphatase and Regulates Phosphate Remobilization in Rice

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Improvement in phosphate acquisition and utilization by a secretory purple acid phosphatase (OsPAP21b) in rice

Phosphate (Pi) deficiency in soil system is a limiting factor for rice growth and yield. Majority of the soil phosphorus (P) is organic in nature, not readily available for root uptake. Low Pi-inducible purple acid phosphatases (PAPs) are hypothesized to enhance the availability of Pi in soil and cellular system. However, information on molecular and physiological roles of rice PAPs is very lim...

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Improving Phosphorus Efficiency in Crops with Focus on Purple Acid Phosphatase: Potentials and Perspective

Low-phosphorus (P) stress as a key factor limiting plant growth and production is common in most agricultural soils. Most of the soil-applied phosphate will be rapidly immobilized and most of annually applied phosphate fertilizers are fixed in the soil in organic forms by adsorption, sedimentation and transformation. However, excess P application may lead to contamination of water sources by en...

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Cloning and characterization of purple acid phosphatase phytases from wheat, barley, maize, and rice.

Barley (Hordeum vulgare) and wheat (Triticum aestivum) possess significant phytase activity in the mature grains. Maize (Zea mays) and rice (Oryza sativa) possess little or virtually no preformed phytase activity in the mature grain and depend fully on de novo synthesis during germination. Here, it is demonstrated that wheat, barley, maize, and rice all possess purple acid phosphatase (PAP) gen...

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Functional Assessment of an Overexpressed Arabidopsis Purple Acid Phosphatase Gene (Atpap26) in Tobacco Plants

Background: Overexpression of known genes encoding key phosphate (Pi)-metabolizing enzymes, such as acid phosphatases (APases), is presumed to help plants with Pi availability and absorption as they are mostly exposed to suboptimal environmental conditions for this vital element.Objectives: In this study, the overexpression effect of AtPAP26, one of the m...

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Reactivity of M(II) metal-substituted derivatives of pig purple acid phosphatase (uteroferrin) with phosphate.

The Fe(II) of the binuclear Fe(II)Fe(III) active site of pig purple acid phosphatase (uteroferrin) has been replaced in turn by five M(II) ions (Mn(II), Co(II), Ni(II), Cu(II), and Zn(II)). An uptake of 1 equiv of M(II) is observed in all cases except that of Cu(II), when a second more loosely bound Cu(II) is removed by treatment with edta. The products have been characterized by different anal...

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ژورنال

عنوان ژورنال: Plant and Cell Physiology

سال: 2017

ISSN: 0032-0781,1471-9053

DOI: 10.1093/pcp/pcx041