First published online June 20, 2002; 10.1104/pp.001909
Plant Physiol, July 2002, Vol. 129, pp. 1320-1329
Salt Induction of Fatty Acid Elongase and Membrane Lipid
Modifications in the Extreme Halotolerant Alga Dunaliella
salina1
Malkit
Azachi,2
Avi
Sadka,3
Morly
Fisher,4
Paulina
Goldshlag,
Irena
Gokhman, and
Ada
Zamir*
Department of Biological Chemistry, Weizmann Institute of Science,
Rehovot 76100, Israel (M.A., A.S., M.F., I.G., A.Z.); and Volcani
Center, Bet Dagan 50250, Israel (P.G.)
In studies of the outstanding salt tolerance of the
unicellular green alga Dunaliella salina, we isolated a
cDNA for a salt-inducible mRNA encoding a protein homologous to plant
-ketoacyl-coenzyme A (CoA) synthases (Kcs). These microsomal enzymes
catalyze the condensation of malonyl-CoA with acyl-CoA, the first and
rate-limiting step in fatty acid elongation. Kcs activity, localized to
a D. salina microsomal fraction, increased in cells
transferred from 0.5 to 3.5 M NaCl, as did the level of the
kcs mRNA. The function of the kcs
gene product was directly demonstrated by the condensing activity
exhibited by Escherichia coli cells expressing the
kcs cDNA. The effect of salinity on kcs
expression in D. salina suggested the possibility that
salt adaptation entailed modifications in the fatty acid composition of
algal membranes. Lipid analyses indicated that microsomes, but not
plasma membranes or thylakoids, from cells grown in 3.5 M
NaCl contained a considerably higher ratio of C18 (mostly unsaturated)
to C16 (mostly saturated) fatty acids compared with cells grown in 0.5 M salt. Thus, the salt-inducible Kcs, jointly with fatty
acid desaturases, may play a role in adapting intracellular membrane
compartments to function in the high internal glycerol concentrations
balancing the external osmotic pressure.
1
This work was supported by Nature Beta
Technologies (Eilat, Israel), by the Nikken-Sohonsha Corporation (Gifu,
Japan), and by the Magnet Program, Israeli Ministry of Industry and Commerce.
2
Present address: Omrix, Weizmann Science Park, Nes-Ziona
76106, Israel.
3
Present address: Volcani Center, Bet Dagan
50250, Israel.
4
Present address: Institute of Biological Research,
Nes-Ziona 74100, Israel.
*
Corresponding author; e-mail bczamir{at}wicc.weizmann.ac.il; fax
972-8-9344118.
© 2002 American Society of Plant Physiologists
This article has been cited by other articles:

|
 |

|
 |
 
A. Katz, P. Waridel, A. Shevchenko, and U. Pick
Salt-induced Changes in the Plasma Membrane Proteome of the Halotolerant Alga Dunaliella salina as Revealed by Blue Native Gel Electrophoresis and Nano-LC-MS/MS Analysis
Mol. Cell. Proteomics,
September 1, 2007;
6(9):
1459 - 1472.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
M. Venegas-Caleron, F. Beaudoin, O. Sayanova, and J. A. Napier
Co-transcribed Genes for Long Chain Polyunsaturated Fatty Acid Biosynthesis in the Protozoon Perkinsus marinus Include a Plant-like FAE1 3-Ketoacyl Coenzyme A Synthase
J. Biol. Chem.,
February 2, 2007;
282(5):
2996 - 3003.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
U. K. Bageshwar, L. Premkumar, I. Gokhman, T. Savchenko, J. L. Sussman, and A. Zamir
Natural protein engineering: a uniquely salt-tolerant, but not halophilic, {alpha}-type carbonic anhydrase from algae proliferating in low- to hyper-saline environments
Protein Eng. Des. Sel.,
February 1, 2004;
17(2):
191 - 200.
[Abstract]
[Full Text]
[PDF]
|
 |
|
|
|