Most transport proteins in plant cells are energized by electrochemical gradients of protons across the plasma membrane. The formation of these gradients is due to the action of plasma membrane H+ pumps fuelled by ATP. The plasma membrane H+-ATPases share a membrane topography and general mechanism of action with other P-type ATPases, but differ in regulatory properties. Recent advances in the field include the identification of the complete H+-ATPase gene family in Arabidopsis, analysis of H+-ATPase function by the methods of reverse genetics, an improved understanding of the posttranslational regulation of pump activity by 14-3-3 proteins, novel insights into the H+ transport mechanism, and progress in structural biology. Furthermore, the elucidation of the three-dimensional structure of a related Ca2+ pump has implications for understanding of structure-function relationships for the plant plasma membrane H+-ATPase.

PLANT PLASMA MEMBRANE H+-ATPases: Powerhouses for Nutrient Uptake.

The plasma membrane

Phosphorus (P) is an essential plant nutrient and one of the most limiting in natural habitats as well as in agricultural production world-wide. The control of P acquisition efficiency and its subsequent uptake and translocation in vascular plants is complex. The physiological role of key cellular structures in plant P uptake and underlying molecular mechanisms are discussed in this review, with emphasis on phosphate transport across the cellular membrane at the root and arbuscular-mycorrhizal (AM) interfaces. The tools of molecular genetics have facilitated novel approaches and provided one of the major driving forces in the investigation of the basic transport mechanisms underlying plant P nutrition. Genetic engineering holds the potential to modify the system in a targeted way at the root-soil or AM symbiotic interface. Such approaches should assist in the breeding of crop plants that exhibit improved P acquisition efficiency and thus require lower inputs of P fertilizer for optimal growth. Whether engineering of P transport systems can contribute to enhanced P uptake will be discussed.

Functional biology of plant phosphate uptake at root and mycorrhiza interfaces

This review deals with aspects of the cellular and molecular biology of the sieve element/companion cell complex, the functional unit of sieve tubes in angiosperms. It includes the following issues: (a) evolution of the sieve elements; (b) the specific structural outfit of sieve elements and its functional significance; (c) modes of cellular and molecular interaction between sieve element and companion cell; (d) plasmodesmal trafficking between sieve element and companion cell as the basis for macromolecular long-distance signalling in the phloem; (e) diversity of sieve element/ companion cell complexes in the respective phloem zones (collection phloem, transport phloem, release phloem); (f) deployment of carriers, pumps and channels on the plasma membrane of sieve element/companion cell complexes in various phloem zones; and (g) implications of the molecular-cellular equipment of sieve element/companion cells complexes for mass flow of water and solutes in a wholeplant frame.

https://onlinelibrary.wiley.com/doi/pdf/10.1046/j.1365-3040.2003.00963.x

The phloem, a miracle of ingenuity

Through form to function: root hair development and nutrient uptake

The plasma membrane H+-ATPase couples ATP hydrolysis to proton transport, thereby establishing the driving force for solute transport across the plasma membrane. In Nicotiana plumbaginifolia, this enzyme is encoded by at least nine pma (plasma membrane H+-ATPase) genes. Four of these are classified into two gene subfamilies, pma1-2-3 and pma4, which are the most highly expressed in plant species. We have isolated genomic clones for pma2 and pma4. Mapping of their transcript 5' end revealed the presence of a long leader that contained small open reading frames, regulatory features typical of other pma genes. The gusA reporter gene was then used to determine the expression of pma2, pma3 and pma4 in N. tabacum. These data, together with those obtained previously for pma1, led to the following conclusions. (i) The four pma-gusA genes were all expressed in root, stem, leaf and flower organs, but each in a cell-type specific manner. Expression in these organs was confirmed at the protein level, using subfamily-specific antibodies. (ii) pma4-gusA was expressed in many cell types and notably in root hair and epidermis, in companion cells, and in guard cells, indicating that in N. plumbaginifolia the same H+-ATPase isoform might be involved in mineral nutrition, phloem loading and control of stomata aperture. (iii) The second gene subfamily is composed, in N. plumbaginifolia, of a single gene (pma4) with a wide expression pattern and, in Arabidopsis thaliana, of three genes (aha1, aha2, aha3), at least two of them having a more restrictive expression pattern. (iv) Some cell types expressed pma2 and pma4 at the same time, which encode H+-ATPases with different enzymatic properties.

Expression analysis of two gene subfamilies encoding the plasma membrane H+‐ATPase in Nicotiana plumbaginifolia reveals the major transport functions of this enzyme

A cDNA clone was isolated for a fourth pma gene encoding a putative plasma membrane H(+)-ATPase of Nicotiana plumbaginifolia. The sequence of the predicted 952 residue PMA4 polypeptide was compared with those of other known plant PMAs, revealing a higher identity with the Arabidopsis thaliana proteins (86-89%) than with the other three N. plumbaginifolia PMA proteins (80-82%). This supports the view that there are two pma subfamilies which probably arose from a gene duplication predating the separation of the Dilleniidae and Asteridae plant subclasses. Measured pma4 transcript levels indicate that pma4 is similarly expressed in root, stem, leaf, and flower tissues, contrary to the pmal-3 subfamily whose members displayed differential expression according to the organ.

Identification and characterization of a second plasma membrane H(+)-ATPase gene subfamily in Nicotiana plumbaginifolia.

Expression analysis of the plasma membrane H+-ATPase pma4 transcription promoter from Nicotiana plumbaginifolia activated by the CaMV 35S promoter enhancer

Luc Moriau

Papers

Expression analysis of two gene subfamilies encoding the plasma membrane H+‐ATPase in Nicotiana plumbaginifolia reveals the major transport functions of this enzyme

Identification and characterization of a second plasma membrane H(+)-ATPase gene subfamily in Nicotiana plumbaginifolia.

Expression analysis of the plasma membrane H+-ATPase pma4 transcription promoter from Nicotiana plumbaginifolia activated by the CaMV 35S promoter enhancer