scholarly journals Ethanol-Induced Injuries to Carrot Cells

1991 ◽  
Vol 95 (3) ◽  
pp. 748-752 ◽  
Author(s):  
Pierdomenico Perata ◽  
Amedeo Alpi
Keyword(s):  
1991 ◽  
Vol 82 (1) ◽  
pp. 103-108
Author(s):  
P. Perata ◽  
A. Alpi

1992 ◽  
Vol 37 (4) ◽  
pp. 296-300
Author(s):  
Kenji Usui ◽  
Jun-ichi Adachi ◽  
Srisom Suwangwong ◽  
Kozo Ishizuka

1997 ◽  
Vol 325 (3) ◽  
pp. 761-769 ◽  
Author(s):  
Isabelle GARCIA ◽  
Matthew RODGERS ◽  
Catherine LENNE ◽  
Anne ROLLAND ◽  
Alain SAILLAND ◽  
...  

p-Hydroxyphenylpyruvate dioxygenase catalyses the transformation of p-hydroxyphenylpyruvate into homogentisate. In plants this enzyme has a crucial role because homogentisate is the aromatic precursor of all prenylquinones. Furthermore this enzyme was recently identified as the molecular target for new families of potent herbicides. In this study we examine precisely the localization of p-hydroxyphenylpyruvate dioxygenase activity within carrot cells. Our results provide evidence that, in cultured carrot cells, p-hydroxyphenylpyruvate dioxygenase is associated with the cytosol. Purification and SDS/PAGE analysis of this enzyme revealed that its activity is associated with a polypeptide of 45–46 kDa. This protein specifically cross-reacts with an antiserum raised against the p-hydroxyphenylpyruvate dioxygenase of Pseudomonas fluorescens. Gel-filtration chromatography indicates that the enzyme behaves as a homodimer. We also report the isolation and nucleotide sequence of a cDNA encoding a carrot p-hydroxyphenylpyruvate dioxygenase. The nucleotide sequence (1684 bp) encodes a protein of 442 amino acid residues with a molecular mass of 48094 Da and shows specific C-terminal regions of similarity with other p-hydroxyphenylpyruvate dioxygenases. This cDNA encodes a functional p-hydroxyphenylpyruvate dioxygenase, as evidenced by expression studies with transformed Escherichia coli cells. Comparison of the N-terminal sequence of the 45–46 kDa polypeptide purified from carrot cells with the deduced peptide sequence of the cDNA confirms that this polypeptide supports p-hydroxyphenylpyruvate dioxygenase activity. Immunodetection studies of the native enzyme in carrot cellular extracts reveal that N-terminal proteolysis occurs during the process of purification. This proteolysis explains the difference in molecular masses between the purified protein and the deduced polypeptide.


1980 ◽  
Vol 45 (1) ◽  
pp. 257-268
Author(s):  
C.W. Lloyd ◽  
S.B. Lowe ◽  
G.W. Peace

The growth regulator 2,4-D (2,4-dichlorophenoxyacetic acid) has been used to investigate the inter-relationship between cell elongation and cell division in carrot suspension cells. Maintained in 1 mg/l. 2,4-D, dividing populations of cells remain spheroidal and in clusters. But when subcultured into lower levels or zero, 2,4-D they increasingly elongate at the expense of division. Over the range of 0 to 1.0 mg/l, 2,4-D, elongation and division are therefore inversely related. However, by suppressing the mitogenic effect with FUdR it can be shown that cells do elongate in 1 mg/l. 2,4-D—a concentration which otherwise produces dividing, spheroidal cells. This indicates that mitogenc levels of 2,4-D do not perturb structures which support cellular elongation. This conclusion is confirmed by immuno- and electron-microscopy which show that development of elaborate arrays of cytoplasmic microtubules is unaffected by 1 mg/l. 2,4-D when FUdR is present. It is concluded that over the time periods under study here, 2,4-D regulates cell size (and shape) by stimulating growing cells to enter the division cycle and not by inhibiting elongation per se.


1981 ◽  
Vol 67 (4) ◽  
pp. 603-607 ◽  
Author(s):  
Michael J. Montague ◽  
Russell K. Enns ◽  
Ned R. Siegel ◽  
Ernest G. Jaworski

1990 ◽  
Vol 96 (4) ◽  
pp. 721-730
Author(s):  
LOUISE COLE ◽  
JULLIAN COLEMAN ◽  
DAVID EVANS ◽  
CHRIS HAWES

The uptake of pure non-conjugated fluorescein isothiocyanate (FITC) and of the membraneimpermeant probe FITC—dextran into suspensioncultured carrot cells and protoplasts has been investigated. Commercial samples of a 70K (K=103Mr) FITC—dextran were shown to contain contaminant FITC and/or its degradation products, which were rapidly internalised into the vacuolar system of both cells and protoplasts. However, purified samples of the 70K FITC—dextran were taken up into the vacuoles of cells but not protoplasts after a lh incubation period. This apparent difference in the ability of cells and protoplasts to internalise FITC—dextrans was confirmed using samples of both commercial and purified 20K FITC—dextran as putative endocytotic probes. Both confocal and conventional fluorescence microscopy of FITC—treated cells have shown that FITC was internalised into similar intracellular compartments as was observed in cells treated with three-times purified 70K FITC—dextran. Thus, FITC was a useful fluorophore for rapidly labelling both the putative endocytotic compartments and the pleiomorphic vacuolar system of carrot cells. Kinetic studies indicated that FITC entered the cell by diffusion in the form of the neutral molecule. We have shown that treatment of cells or protoplasts with the drug Probenecid reversibly inhibited the uptake of FITC from the cytoplasm into the vacuole. In addition, the uptake of FITC into isolated vacuoles was enhanced in the presence of Mg-ATP


Author(s):  
C. Lennel ◽  
M. Matringe ◽  
A. Rolland ◽  
A. Sailland ◽  
K. E. Pallett ◽  
...  

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