Visualization of actin cytoskeletal dynamics during the cell cycle in tobacco (Nicotiana tabacum L. cv Bright Yellow) cells

2006 ◽  
Vol 98 (5) ◽  
pp. 295-306 ◽  
Author(s):  
Miaomiao Yu ◽  
Ming Yuan ◽  
Haiyun Ren
Keyword(s):  
Cell Cycle ◽  
Nicotiana Tabacum ◽  
Bright Yellow ◽  
Nicotiana Tabacum L ◽  
Cytoskeletal Dynamics ◽  
Actin Cytoskeletal Dynamics

scholarly journals Identification of a Cell Cycle-Related Gene, Cyclin, in Nicotiana tabacum (L.)

1995 ◽  
Vol 108 (1) ◽  
pp. 425-426 ◽  
Author(s):  
L. X. Qin ◽  
L. Richard ◽  
C. Perennes ◽  
P. Gadal ◽  
C. Bergounioux
Keyword(s):  
Cell Cycle ◽  
Nicotiana Tabacum ◽  
Related Gene ◽  
Nicotiana Tabacum L ◽  
Cell Cycle Related Gene ◽  
A Cell

Copper-mediated oxidative burst in Nicotiana tabacum L. cv. Bright Yellow 2 cell suspension cultures

PROTOPLASMA ◽  
2003 ◽  
Vol 221 (1-2) ◽  
pp. 93-100 ◽  
Author(s):  
T. Raeymaekers ◽  
G. Potters ◽  
H. Asard ◽  
Y. Guisez ◽  
N. Horemans
Keyword(s):  
Nicotiana Tabacum ◽  
Cell Suspension ◽  
Oxidative Burst ◽  
Cell Suspension Cultures ◽  
Suspension Cultures ◽  
Bright Yellow ◽  
Nicotiana Tabacum L

scholarly journals Alamethicin permeabilizes the plasma membrane and mitochondria but not the tonoplast in tobacco (Nicotiana tabacum L. cv Bright Yellow) suspension cells

2005 ◽  
Vol 389 (3) ◽  
pp. 695-704 ◽  
Author(s):  
Sandra Matic ◽  
Daniela A. Geisler ◽  
Ian M. Møller ◽  
Susanne Widell ◽  
Allan G. Rasmusson
Keyword(s):  
Nicotiana Tabacum ◽  
Plasma Membranes ◽  
Animal Cells ◽  
Suspension Cells ◽  
Respiratory Enzymes ◽  
Mitochondrial Oxygen Consumption ◽  
Permeabilized Cells ◽  
Bright Yellow ◽  
Transport Chain ◽  
Nicotiana Tabacum L

The ion channel-forming peptide AlaM (alamethicin) is known to permeabilize isolated mitochondria as well as animal cells. When intact tobacco (Nicotiana tabacum L.) Bright Yellow-2 cells were treated with AlaM, the cells became permeable for low-molecular-mass molecules as shown by induced leakage of NAD(P)+. After the addition of cofactors and substrates, activities of cytosolic as well as mitochondrial respiratory enzymes could be directly determined inside the permeabilized cells. However, at an AlaM concentration at which the cytoplasmic enzymes were maximally accessible, the vacuole remained intact, as indicated by an unaffected tonoplast proton gradient. Low-flux permeabilization of plasma membranes and mitochondria at moderate AlaM concentrations was reversible and did not affect cell vigour. Higher AlaM concentrations induced cell death. After the addition of catalase that removes the H2O2 necessary for NADH oxidation by apoplastic peroxidases, mitochondrial oxygen consumption could be measured in permeabilized cells. Inhibitor-sensitive oxidation of the respiratory substrates succinate, malate and NADH was observed after the addition of the appropriate coenzymes (ATP, NAD+). The capacities of different pathways in the respiratory electron-transport chain could thus be determined directly. We conclude that AlaM permeabilization provides a very useful tool for monitoring metabolic pathways or individual enzymes in their native proteinaceous environment with controlled cofactor concentrations. Possible uses and limitations of this method for plant cell research are discussed.

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