These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Expression of the gene for the delta9 acyl-lipid desaturase in the thermophilic cyanobacterium.
    Author: Kiseleva LL, Serebriiskaya TS, Horvàth I, Vigh L, Lyukevich AA, Los DA.
    Journal: J Mol Microbiol Biotechnol; 2000 Jul; 2(3):331-8. PubMed ID: 10937442.
    Abstract:
    A single-copy gene resembling the gene for the delta9 acyl-lipid desaturase (desC) was cloned from the thermophilic cyanobacterium Synechococcus vulcanus. Expression of desC in Escherichia coli confirmed that it encodes the delta9 desaturase. The nucleotide sequence of the desC was characterized by high G+C content that is typical of the sequences of thermophilic bacteria. The deduced amino acid sequence exhibited low Cys content and high Arg/Lys ratio that are the attributes of thermostable enzymes. A low level of the desC mRNA was detected in the cells grown at 55 degrees C, the optimum growth temperature for S. vulcanus. About a 10-fold increase was observed in the levels of the transcript and the protein during the shift in temperature from 55 to 45 degrees C. At 35 degrees C the amount of the desC mRNA and of the enzyme accumulated in the cells, was 3 to 4 times smaller than at 45 degrees C. At both temperatures, however, lipids were desaturated at similar rates. These results suggest that in S. vulcanus the conversion of stearic acid into oleic acid may be controlled not only by the de novo synthesis of the delta9 desaturase but, possibly, by the activation of the pre-existing enzyme.
    [Abstract] [Full Text] [Related] [New Search]