Structure of a cDNA for an acid phosphatase from phosphate-deficient lupin (<i>Lupinus albus</i>L.) Roots

Wasaki, Jun; Omura, Masanori; Osaki, Mitsuru; Ito, Hiroyuki; Matsui, Hirokazu; Shinano, Takuro; Tadano, Toshiaki

doi:10.1080/00380768.1999.10409358

Cited by 45 publications

(22 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One PAP from Spirodela oligorrhiza has been found to be glycosylphosphatidylinositol anchored in the cell (24). Another PAP from Lupinus albus may contain a third domain (with a structure resembling that of sterol desaturases) at the carboxyl terminus (25,26). It is not known how common the latter two forms of posttranslational modification are in PAPs from other species.…”

Section: The Nucleotide Sequence(s) Reported In This Paper Has Been Smentioning

confidence: 95%

“…In higher plants, PAPs have mostly been studied for their potential involvement in phosphorus nutrition because their hydrolytic activity may aid the release of inorganic P (P i ) from organic P that is not readily available to plant cells. Two PAPs (secreted PAP, membrane PAP) from L. albus have been shown to be highly inducible by phosphate deprivation (25,26). The induction and secretion of secreted PAP are specific to proteoid roots, a structure that is specifically formed in L. albus as one of the adaptations to phosphorus deficiency, indicating that, at least in this species, PAPs may play an important part in phosphorus nutrition (26,30).…”

Section: The Nucleotide Sequence(s) Reported In This Paper Has Been Smentioning

confidence: 99%

See 1 more Smart Citation

Purple Acid Phosphatases of Arabidopsis thaliana

Li¹,

Zhu²,

Liu³

et al. 2002

Journal of Biological Chemistry

252

130

View full text Add to dashboard Cite

Purple acid phosphatases (PAPs) are members of the metallo-phosphoesterase family. They are characterized by the presence of seven conserved amino acid residues involved in coordinating the dimetal nuclear center in their reactive site. We compared the 29 PAPs predicted for Arabidopsis thaliana in their varieties of potential metal-ligating residues. Although 24 members possessed sets of metal-ligating residues typical of known PAPs, 1 member lacked four of the seven residues. For the remaining four members, potential metal-ligating residues were generally more similar to those in metal-dependent exonucleases and related proteins. Evidence was obtained for the expression of the majority of the 29 PAPs. To facilitate future investigations, a scheme for naming Arabidopsis PAPs and a system for classifying the 29 PAPs are proposed. The cDNA sequences and the responses to phosphate deprivation of seven Arabidopsis PAPs (AtPAP7-AtPAP13) were characterized. For some AtPAPs analyzed, there were fully processed transcripts as well as splice variants. The splice variants of AtPAP10 were found to associate with polyribosomes and may be translated into a NH 2 -terminal truncated protein. Phylogenetic investigations showed that AtPAPs 7 and 8, together with similar enzymes from other plant species, formed the low molecular weight plant PAP group. Members of this group were more closely related to PAPs from mammalian cells. AtPAPs 9 -13, together with kidney bean PAP, formed the high molecular weight PAP group. In phosphate deprivation experiments, gene transcription of AtPAP11 and AtPAP12 was induced and increased, respectively, whereas that of the remaining five AtPAPs was not affected by phosphate deprivation. The present work demonstrates that structure variation and expression regulation of plant PAPs are more complex than previously described and provides a framework for comprehensive molecular genetic and biochemical studies of all Arabidopsis PAPs in the future.

show abstract

Section: The Nucleotide Sequence(s) Reported In This Paper Has Been Smentioning

confidence: 95%

Section: The Nucleotide Sequence(s) Reported In This Paper Has Been Smentioning

confidence: 99%

Purple Acid Phosphatases of Arabidopsis thaliana

Li¹,

Zhu²,

Liu³

et al. 2002

Journal of Biological Chemistry

252

130

View full text Add to dashboard Cite

show abstract

“…A wide range of plant species secretes acid phosphatase into rhizosphere under P-deficient conditions irrespective of mycotrophic status. Lupinus albus secretes substantial amounts of acid phosphatase from proteoid (cluster) roots formed under P stress (Miller et al 2001;Wasaki et al 1999). Since L. albus does not form mycorrhiza, the secretion of acid phosphatase is regarded as an important part of P acquisition strategies of nonmycorrhizal plants.…”

Section: Discussionmentioning

confidence: 99%

A New Hypothesis on the Strategy for Acquisition of Phosphorus in Arbuscular Mycorrhiza: Up-Regulation of Secreted Acid Phosphatase Gene in the Host Plant

Ezawa¹,

Hayatsu²,

Saitô³

2005

MPMI

View full text Add to dashboard Cite

The mycorrhiza-responsive phosphatase of Tagetes patula in symbiosis with Glomus etunicatum was detected by electrophoresis, was purified by column chromatography, and was characterized as acid phosphatase that was secreted into rhizosphere. The N-terminal amino acid sequence was determined by a gas-phase sequencer, and a cDNA fragment of the phosphatase gene (TpPAP1) was amplified by degenerate primers designed based on the N-terminal amino acid sequence. The full-length cDNA was obtained by the rapid amplification of cDNA ends technique. The TpPAP1 was of host origin, and the cDNA was 1,843 bp long with a predicted open reading frame of polypeptide of 466 amino acids. Phylogenetic analysis revealed that the gene fell into the cluster of plant high-molecular-weight purple acid phosphatase. Expression analysis of the TpPAP1 in T. patula in symbiosis with Archaeospora leptoticha showed that the levels of transcripts increased eightfold by mycorrhizal colonization. Western blot analysis revealed that the 57-kDa protein corresponding to the mycorrhiza-responsive phosphatase increased by mycorrhizal colonization. The present study proposes a new strategy for acquisition of P in arbuscular mycorrhizal associations in which the fungal partner activates a part of the low-P adaptation system of the plant partner, phosphatase secretion, and improves the overall efficiency of P uptake.

show abstract

“…This result suggests a binding of phosphatases to plasma membrane. In white lupin, cDNA clones of two isoforms of acid phosphatases, lasap1 and lasap2, have been characterized (Wasaki et al, 1999(Wasaki et al, , 2000. lasap2 is specifically expressed in roots exposed to P deficiency and is supposed to encode secretory acid phosphatase.…”

Section: Isolation Of Plasma Membrane From Different Types Of White Lmentioning

confidence: 99%

Adaptation of H+-Pumping and Plasma Membrane H+ ATPase Activity in Proteoid Roots of White Lupin under Phosphate Deficiency

et al. 2002

View full text Add to dashboard Cite

White lupin (Lupinus albus) is able to adapt to phosphorus deficiency by producing proteoid roots that release a huge amount of organic acids, resulting in mobilization of sparingly soluble soil phosphate in rhizosphere. The mechanisms responsible for the release of organic acids by proteoid root cells, especially the trans-membrane transport processes, have not been elucidated. Because of high cytosolic pH, the release of undissociated organic acids is not probable. In the present study, we focused on H ϩ export by plasma membrane H ϩ ATPase in active proteoid roots. In vivo, rhizosphere acidification of active proteoid roots was vanadate sensitive. Plasma membranes were isolated from proteoid roots and lateral roots from P-deficient and -sufficient plants. In vitro, in comparison with two types of lateral roots and proteoid roots of P-sufficient plants, the following increase of the various parameters was induced in active proteoid roots of P-deficient plants: (a) hydrolytic ATPase activity, (b) V max and K m , (c) H ϩ ATPase enzyme concentration of plasma membrane, (d) H ϩ -pumping activity, (e) pH gradient across the membrane of plasmalemma vesicles, and (f) passive H ϩ permeability of plasma membrane. In addition, lower vanadate sensitivity and more acidic pH optimum were determined for plasma membrane ATPase of active proteoid roots. Our data support the hypothesis that in active proteoid root cells, H ϩ and organic anions are exported separately, and that modification of plasma membrane H ϩ ATPase is essential for enhanced rhizosphere acidification by active proteoid roots.P is one of the most important plant nutrients that significantly affect growth and metabolism. Although the total amount of P in soil may be high, it is often present in unavailable forms such as phytic acid (Richardson, 1994), or Ca, Fe, and Al phosphates (Holford, 1997). Low availability of P is a major constraint for crop production in many low-input systems of agriculture worldwide, especially in the highly weathered soils of the humid tropics and subtropics, in many sandy soils of the semiarid tropics, and in calcareous soils of the temperate regions, where crop productivity is severely compromised through lack of available P (Raghothama, 1999). Also, after application of P to the soil the recovery of applied P by crop plants in a growing season is very low, because in the soil more than 80% of the P becomes immobile and unavailable for plant uptake due to adsorption on Al or Fe oxides/hydroxides, precipitation with Ca, or conversion to organic forms (Holford, 1997).Higher plants have developed various strategies of acquiring sparingly soluble nutrients from soil. In response to P deficiency, various species from different families develop so-called proteoid roots. These are bottlebrush-like clusters of rootlets of limited growth with an average length of 0.5 to 1 cm. The rootlets are closely arranged along lateral roots and are usually covered with long and dense root hairs (Purnell, 1960; Dinkelaker et al., 1995;Watt and Evans...

show abstract

Structure of a cDNA for an acid phosphatase from phosphate-deficient lupin (Lupinus albusL.) Roots

Cited by 45 publications

References 27 publications

Purple Acid Phosphatases of Arabidopsis thaliana

Purple Acid Phosphatases of Arabidopsis thaliana

A New Hypothesis on the Strategy for Acquisition of Phosphorus in Arbuscular Mycorrhiza: Up-Regulation of Secreted Acid Phosphatase Gene in the Host Plant

Adaptation of H+-Pumping and Plasma Membrane H+ ATPase Activity in Proteoid Roots of White Lupin under Phosphate Deficiency

Contact Info

Product

Resources

About