Ion Uptake and Protein Synthesis in Enzymatically Isolated Plant Cells

Nature ◽  
1965 ◽  
Vol 205 (4974) ◽  
pp. 921-922 ◽  
Author(s):  
W. H. JYUNG ◽  
S. H. WITTWER ◽  
M. J. BUKOVAC
Keyword(s):  
Protein Synthesis ◽  
Plant Cells ◽  
Ion Uptake

Protein synthesis and freezing tolerance in plant cells

1988 ◽  
Vol 7 (4) ◽  
pp. 279-302 ◽  
Author(s):  
Anne M. Johnson‐Flanagan ◽  
Jas Singh ◽  
Norman P.A. Huner
Keyword(s):  
Protein Synthesis ◽  
Freezing Tolerance ◽  
Plant Cells

Connexion between Protein Synthesis and Salt Absorption in Plant Cells

Nature ◽  
1962 ◽  
Vol 195 (4845) ◽  
pp. 1014-1014 ◽  
Author(s):  
B. JACOBY ◽  
J. F. SUTCLIFFE
Keyword(s):  
Protein Synthesis ◽  
Plant Cells ◽  
Salt Absorption

Inhibition of Protein Synthesis in Chloroplasts from Plant Cells by Virginiamycin

1979 ◽  
Vol 34 (12) ◽  
pp. 1195-1198 ◽  
Author(s):  
C. Cocito ◽  
O. Tiboni ◽  
F. Vanlinden ◽  
O. Ciferri
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Synergistic Effect ◽  
Plant Cells ◽  
Inhibitory Effect ◽  
Spinach Chloroplasts ◽  
Inhibition Of Protein Synthesis ◽  
Isolated Chloroplasts

Abstract The light-driven incorporation of amino acids by isolated spinach chloroplasts is inhibited by the M component (VM) and not by the S component (VS) of virginiamycin. This inhibitory effect is partially reversible. In chloroplast extracts, poly(U)-directed polyphenylalanine formation is strongly inhibited by VM and not by VS. The in vivo synergistic effect of VM and VS observed in bacteria and algae, does not occur in isolated chloroplasts and chloroplast extracts.

scholarly journals Hormonal regulation of protein synthesis associated with salt tolerance in plant cells

1987 ◽  
Vol 84 (3) ◽  
pp. 739-743 ◽  
Author(s):  
N. K. Singh ◽  
P. C. LaRosa ◽  
A. K. Handa ◽  
P. M. Hasegawa ◽  
R. A. Bressan
Keyword(s):  
Protein Synthesis ◽  
Salt Tolerance ◽  
Hormonal Regulation ◽  
Plant Cells

scholarly journals PINOCYTOSIS, ATP-ASE AND ION UPTAKE BY PLANT CELLS

1973 ◽  
Vol 72 (6) ◽  
pp. 1281-1291 ◽  
Author(s):  
D. A. BAKER ◽  
J. L. HALL
Keyword(s):  
Plant Cells ◽  
Ion Uptake

Can Externally Applied Atp Supply Energy to Active Ion Uptake Mechanisms of Intact Plant Cells?

1974 ◽  
Vol 1 (2) ◽  
pp. 211 ◽  
Author(s):  
U Lüttge ◽  
EV Schöch ◽  
E Ball
Keyword(s):  
External Medium ◽  
Divalent Cations ◽  
Plant Cells ◽  
Bundle Sheath ◽  
Metabolic Inhibition ◽  
Ion Uptake ◽  
Intact Plant ◽  
K Uptake ◽  
Atp Supply ◽  
Uptake Mechanisms

ATP applied in the external medium of leaf slices and bundle-sheath preparations at concentrations between 1.0 and 2.5 mM apparently enhances K+ uptake. However, this effect depends on the presence of Ca2+ or Mg2+ in the medium. ATP is shown to release a Ca2+ or Mg2+ inhibition of K+ uptake. If the Ca2+ or Mg2+ content of the medium is varied and EDTA used to mimic the effect of ATP, it can be demonstrated that the observed effect of ATP is entirely explicable by its chelation of divalent cations. Externally applied ATP has similar relative effects on K+ uptake under control conditions and under conditions where metabolism is inhibited, and although it apparently fully releases metabolic inhibition, these experiments reveal ambiguities which are discussed. It is con- cluded that apparent effects of externally applied ATP may often be indirect. The possibility of specific, i.e. energy-providing, effects can nevertheless not be ruled out in principle, but more sophisti- cated experimentation than found hitherto in the literature is required to demonstrate such effects.

Ion Uptake and Transport through Barley Seedlings: Differential Effect of Cycloheximide

1973 ◽  
Vol 28 (7-8) ◽  
pp. 434-436 ◽  
Author(s):  
André Läuchli ◽  
Ulrich Lüttge ◽  
Michael G. Pitman
Keyword(s):  
Protein Synthesis ◽  
Ion Transport ◽  
Differential Effect ◽  
Ion Uptake ◽  
K Uptake ◽  
Root Cells ◽  
Symplasmic Transport ◽  
Vesicular Secretion ◽  
Uptake And Transport

Cycloheximide inhibits transport of K through barley roots without affecting K uptake and accumulation in the root cells. The inhibitor acts upon protein synthesis but does not appear to uncouple respiration. Requirement of protein synthesis for ion transport through roots is possibly due to involvement of symplasmic transport or vesicular secretion into the xylem.

scholarly journals Polarized localization and borate-dependent degradation of the Arabidopsis borate transporter BOR1 in tobacco BY-2 cells

F1000Research ◽  
2013 ◽  
Vol 2 ◽  
pp. 185 ◽  
Author(s):  
Noboru Yamauchi ◽  
Tadashi Gosho ◽  
Satoru Asatuma ◽  
Kiminori Toyooka ◽  
Toru Fujiwara ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Plasma Membrane ◽  
Degradation Rate ◽  
Degradation Mechanism ◽  
Plant Cells ◽  
High Concentration ◽  
Root Cells ◽  
Gfp Fluorescence ◽  
Specific Degradation ◽  
Transformed Tobacco

In Arabidopsis the borate transporter BOR1, which is located in the plasma membrane, is degraded in the presence of excess boron by an endocytosis-mediated mechanism. A similar mechanism was suggested in rice as excess boron decreased rice borate transporter levels, although in this case whether the decrease was dependent on an increase in degradation or a decrease in protein synthesis was not elucidated. To address whether the borate-dependent degradation mechanism is conserved among plant cells, we analyzed the fate of GFP-tagged BOR1 (BOR1-GFP) in transformed tobacco BY-2 cells. Cells expressing BOR1-GFP displayed GFP fluorescence at the plasma membrane, especially at the membrane between two attached cells. The plasma membrane signal was abolished when cells were incubated in medium with a high concentration of borate (3 to 5 mM). This decrease in BOR1-GFP signal was mediated by a specific degradation of the protein after internalization by endocytosis from the plasma membrane. Pharmacological analysis indicated that the decrease in BOR1-GFP largely depends on the increase in degradation rate and that the degradation was mediated by a tyrosine-motif and the actin cytoskeleton. Tyr mutants of BOR1-GFP, which has been shown to inhibit borate-dependent degradation in Arabidopsis root cells, did not show borate-dependent endocytosis in tobacco BY-2 cells. These findings indicate that the borate-dependent degradation machinery of the borate transporter is conserved among plant species.

scholarly journals EFFECTS OF 60COBALT IONIZING IRRADIATION ON GROWTH AND POLYSOME CONTENT IN PISUM SATIVUM L. `ALASKA'

HortScience ◽  
1992 ◽  
Vol 27 (12) ◽  
pp. 1261d-1261
Author(s):  
Jody A. Goodrich
Keyword(s):  
Protein Synthesis ◽  
Pisum Sativum ◽  
Plant Cells ◽  
Root Tip ◽  
Nuclear Accidents ◽  
Ionizing Irradiation ◽  
Pisum Sativum L ◽  
Living Organisms ◽  
Injurious Effects

This research tested the hypothesis that 60Co ionizing irradiation degrades polysomes to monosomes, a process that reduces growth of Pisum sativum seedlings. Dry and imbibed seeds and 5-day-old seedlings were exposed to 1.8, 3.6, 7.2, 14.4, or 28.8 krad of 60Co irradiation. Immediately after irradiation treatments, dry and imbibed seeds were planted, and later seedlings were harvested and analyzed. Five 1-cm root-tip samples from 5-day-old seedlings were crushed and layered onto 15% to 60% sucrose gradients and centrifuged for 55 min. The samples were processed through an ISCO ultraviolet chart maker. The monosome and polysome weights were read and analyzed. The monosome content was greater in the irradiated 5-day-old seedlings than in seedlings from dry and imbibed seeds. The growth of 5-day-old irradiated seedlings and seedlings from imbibed seeds was less than that of seedlings from dry seeds. The reduced growth of the irradiated seedlings suggests damage to the polysomes. When protein synthesis in plant cells is altered, perhaps through RNA decoding mechanisms, growth may be partially or completely arrested. Using sensitive plants to establish the injurious effects of ionizing irradiation on living organisms can educate and alert society to the detrimental effects of overexposure to irradiation such as that caused by nuclear accidents.

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