P-ring: The conserved nature of phosphorus enriched cells in seedling roots of distantly related species.

Plants require sunlight, carbon dioxide, water and mineral ions for their growth and development. Roots in vascular plants sequester water and ions from soil and transport them to the aboveground parts of the plant. Due to heterogeneous nature of soil, roots have evolved several regulatory barriers from molecular to organismic level that selectively allows certain ions to enter the vascular tissues for transport according to the physiological and metabolic demands of plant cell. Current literature profusely elaborates about apoplastic barriers, but the possibility of the existence of a symplastic regulation through phosphorous-enriched cells has not been mentioned. Recent investigations on native ion distribution in seedling roots of several species (Pinus pinea, Zea mays and Arachis hypogaea) identified an ionomic structure termed as "P-ring". The P-ring is composed of a group of phosphorous-rich cells arranged in radial symmetry encircling the vascular tissues. Physiological investigations indicate that the structure is relatively inert to external temperature and ion fluctuations while anatomical studies indicates that they are less likely to be apoplastic in nature. Furthermore, their localization surrounding vascular tissues and in evolutionarily distinct plant lineages might indicate their conserved nature and involvement in ion regulation. Undoubtedly, this is an interesting and important observation that has significant merit for further investigations by the plant science community.

Tissue accumulation patterns and concentrations of potassium, phosphorus, and carboxyfluorescein translocated from pine seed to the root.

MAIN CONCLUSION: Potassium (K), phosphorous (P), and carboxyfluorescein (CF) accumulate in functionally distinct tissues within the pine seedling root cortex. Seedlings of Pinus pinea translocate exogenous CF and endogenous K and P from the female gametophyte/cotyledons to the growing radicle. Following unloading in the root tip, these materials accumulate in characteristic spatial patterns. Transverse sections of root tips show high levels of P in a circular ring of several layers of inner cortical cells. K and CF are minimal in the high P tissue. In contrast, high levels of K and CF accumulate in outer cortical cells, and in the vascular cylinder. These patterns are a property of living tissue because they change after freeze-thaw treatment, which kills the cells and results in uniform distribution of K and P. K concentration can be reduced to undetectable levels by incubation of roots in 100 mM NaCl. Inductively coupled plasma optical emission spectrometry (ICP-OES) analysis and scanning electron microscopy (SEM)/energy-dispersive X-ray spectroscopy (EDS) of root segments both reliably determine K and P concentrations.

F-actin distribution in root primary tissues of several seed plant species.

PREMISE OF THE STUDY: Primary vascular tissues of angiosperm and gymnosperm roots have significant anatomical differences. In gymnosperms, lack of protophloem sieve elements indicates a lengthy parenchymatous pathway for nutrient transport to the root apical meristem (RAM). Because F-actin is an essential component of transport in parenchyma cells, the distribution of F-actin was determined and compared among roots of several angiosperm and gymnosperm species. METHODS: Roots were chemically fixed and sectioned by hand to enable rapid production of many sections for labeling F-actin with phalloidin. KEY RESULTS: In angiosperm and gymnosperm root tips, relative intensity of F-actin labeling was highest in primary vascular tissues. Parenchyma cells in and around protophloem tended to have more F-actin while cells in cortical and protoxylem tissues tended to have less. In gymnosperms, phloem parenchyma was intensely labeled for several millimeters distal to the root apical meristem (RAM), and the F-actin is mostly composed of bundles that lie parallel to the root longitudinal axis. This orientation differed from the multidirectional arrangement of F-actin filaments in cortical cells. In angiosperms, intense F-actin labeling of pericycle and phloem parenchyma cells occurred around the first mature sieve elements. CONCLUSIONS: F-actin is concentrated in the vascular cylinder, commonly in primary phloem parenchyma. In gymnosperms, the absence of sieve elements suggests that cytoplasmic streaming has a role in some aspect of phloem transport or unloading. In angiosperms, the region of intense F-actin labeling in the phloem parenchyma is limited to the extreme terminal portion of primary phloem where unloading of the earliest mature sieve elements occurs.

Effects of copper on osmoregulation in sheepshead minnow, Cyprinodon variegatus acclimated to different salinities.

The sheepshead minnow, Cyprinodon variegatus is a euryhaline fish that inhabits estuaries and coastal marshes where it encounters a wide range of salinities. Many of these areas also have elevated levels of contaminants, creating the potential for toxic ions to interfere with the uptake of ions for osmoregulation. To determine whether the effect of copper on osmoregulatory activity is dependent on the osmotic conditions that individuals have been living at, fish were acclimated for 14 days to 2.5, 10.5 or 18.5 ppt seawater and then exposed to a fixed free cupric ion level (14.6 µM Cu2+) for 6 h. Plasma Na, plasma Cl, wet/dry weight ratio, transepithelial potential difference (TEPD) and branchial Na(+)/K(+)-ATPase activity were determined before and after copper exposure. We also computed Na and Cl equilibrium potentials. Following the salinity acclimation (in fish not yet exposed to copper), fish from the low salinity group (2.5 ppt) had lower TEPD, lower plasma Na levels and higher branchial Na(+)/K(+)-ATPase activity compared to the fish acclimated to higher salinities. No differences in plasma Cl and wet/dry weight ratio were detected. Copper exposure caused a significant decrease in plasma Na levels and Na(+)/K(+)-ATPase activity and an increase in wet/dry weight ratio, but these changes were limited to the 2.5 ppt salinity group. No significant changes in plasma Cl were detected. Copper treatment resulted in a small decrease in TEPD for all except the lowest salinity acclimation group. A comparison of equilibrium potentials with TEPD showed evidence of active transport of both Na and Cl in 2.5 ppt acclimated fish but not for the 10.5 or the 18.5 ppt acclimated fish. Our results show that effects of copper on osmoregulation are dependent on the fish' past salinity regime, and that these effects tend to be more pronounced for euryhaline fish that have been living under hyposmotic conditions.

A subclass of myosin XI is associated with mitochondria, plastids, and the molecular chaperone subunit TCP-1alpha in maize.

The role and regulation of specific plant myosins in cyclosis is not well understood. In the present report, an affinity-purified antibody generated against a conserved tail region of some class XI plant myosin isoforms was used for biochemical and immunofluorescence studies of Zea mays. Myosin XI co-localized with plastids and mitochondria but not with nuclei, the Golgi apparatus, endoplasmic reticulum, or peroxisomes. This suggests that myosin XI is involved in the motility of specific organelles. Myosin XI was more than 50% co-localized with tailless complex polypeptide-1alpha (TCP-1alpha) in tissue sections of mature tissues located more than 1.0 mm from the apex, and the two proteins co-eluted from gel filtration and ion exchange columns. On Western blots, TCP-1alpha isoforms showed a developmental shift from the youngest 5.0 mm of the root to more mature regions that were more than 10.0 mm from the apex. This developmental shift coincided with a higher percentage of myosin XI /TCP-1alpha co-localization, and faster degradation of myosin XI by serine protease. Our results suggest that class XI plant myosin requires TCP-1alpha for regulating folding or providing protection against denaturation.

Cotton-fiber germin-like protein. II: Immunolocalization, purification, and functional analysis.

Cotton (Gossypium hirsutum L.) contains a germin-like protein (GLP), GhGLP1, that shows tissue-specific accumulation in fiber. The fiber GLP is an oligomeric, glycosylated protein with a subunit size of approximately 25.5 kDa. Accumulation of GhGLP1 occurs during the period of fiber elongation [4-14 days post-anthesis (DPA)]. During early phases of fiber development (2-4 DPA), GhGLP1 localizes to cytoplasmic vesicles as shown by confocal immunofluorescent microscopy. In slightly older fibers (7-10 DPA), GhGLP1 localizes to the apoplast. In other plants, germins and GLPs have been reported to have enzymatic activities including oxalate oxidase (OxO), superoxide dismutase, and ADP-glucose pyrophosphatase. Cotton fiber extracts did not contain OxO activity, nor did intact fibers stain for OxO activity. A four-step purification protocol involving ammonium sulfate precipitation of a 1.0 M NaCl extract, ion-exchange chromatography on DEAE-Trisacryl M, lectin-affinity chromatography, and gel filtration chromatography resulted in electrophoretically pure GhGLP1. While 1.0 M NaCl extracts from 10-14 DPA fiber contained superoxide dismutase and phosphodiesterase activities, GhGLP1 could be separated from both enzyme activities by the purification protocol. Although a GLP accumulates in the cotton fiber apoplast during cell elongation, the function of this protein in fiber growth and development remains unknown.