|
THE PLANT CELL, Vol 1, Issue 2 181-190, Copyright © 1989 by American Society of Plant Biologists
Tomato Hydroxymethylglutaryl-CoA Reductase is Required Early in Fruit Development but not during Ripening
J. O. Narita and W. Gruissem
Department of Botany, University of California, Berkeley, California, 94720
The activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGR) and
the level of its mRNA have been determined at various stages of tomato
fruit development. The HMGR reaction makes mevalonate, a necessary
component in the synthesis of all isoprene containing compounds, such as
sterols and carotenoids. A cDNA clone encoding the active site region of
HMGR has been isolated from a tomato library derived from young-fruit mRNA.
The clone hybridizes to a one- or two-copy fragment in high-stringency DNA
gel blot analyses and detects an mRNA of approximately 3.0 kb. Both HMGR
activity and mRNA levels are high in early stages of tomato fruit
development, when rapid cell division occurs, as well as in the subsequent
early stages of cellular expansion. In contrast, ripening fruit have very
low levels of reductase activity and mRNA, even though large amounts of the
carotenoid lycopene are synthesized during this period. Furthermore, in
vivo inhibition of HMGR during early fruit stages disrupts subsequent
development, whereas inhibition during later stages of fruit expansion has
no apparent effect on ripening. We conclude that the pool of mevalonate
responsible for the synthesis of phytosterols is synthesized primarily
during the first half of tomato fruit development. In addition, the final
period of fruit expansion and ripening is not dependent upon HMGR activity,
but instead utilizes a preexisting pool of pathway intermediates or
requires the use of salvage pathways in the cell.
This article has been cited by other articles:

|
 |

|
 |
 
A. Hemmerlin, J.-F. Hoeffler, O. Meyer, D. Tritsch, I. A. Kagan, C. Grosdemange-Billiard, M. Rohmer, and T. J. Bach
Cross-talk between the Cytosolic Mevalonate and the Plastidial Methylerythritol Phosphate Pathways in Tobacco Bright Yellow-2 Cells
J. Biol. Chem.,
July 11, 2003;
278(29):
26666 - 26676.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
T. P. Devarenne, A. Ghosh, and J. Chappell
Regulation of Squalene Synthase, a Key Enzyme of Sterol Biosynthesis, in Tobacco
Plant Physiology,
July 1, 2002;
129(3):
1095 - 1106.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
S. E. Berdy, J. Kudla, W. Gruissem, and G. E. Gillaspy
Molecular Characterization of At5PTase1, an Inositol Phosphatase Capable of Terminating Inositol Trisphosphate Signaling
Plant Physiology,
June 1, 2001;
126(2):
801 - 810.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
J. Gaffe, J.-P. Bru, M. Causse, A. Vidal, L. Stamitti-Bert, J.-P. Carde, and P. Gallusci
LEFPS1, a Tomato Farnesyl Pyrophosphate Gene Highly Expressed during Early Fruit Development
Plant Physiology,
August 1, 2000;
123(4):
1351 - 1362.
[Abstract]
[Full Text]
|
 |
|

|
 |

|
 |
 
M. Rodríguez-Concepción and W. Gruissem
Arachidonic Acid Alters Tomato HMG Expression and Fruit Growth and Induces 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase-Independent Lycopene Accumulation
Plant Physiology,
January 1, 1999;
119(1):
41 - 48.
[Abstract]
[Full Text]
|
 |
|

|
 |

|
 |
 
W. H. Engfelt, J. E. Shackelford, N. Aboushadi, N. Jessani, K. Masuda, V. G. Paton, G.-A. Keller, and S. K. Krisans
Characterization of UT2 Cells. THE INDUCTION OF PEROXISOMAL 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE
J. Biol. Chem.,
September 26, 1997;
272(39):
24579 - 24587.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
C. J. Denbow, S. Lång, and C. L. Cramer
The N-terminal Domain of Tomato 3-Hydroxy-3-methylglutaryl-CoA Reductases
J. Biol. Chem.,
April 19, 1996;
271(16):
9710 - 9715.
[Abstract]
[Full Text]
[PDF]
|
 |
|
|
|