[Comparative expression in Escherichia coli of the native and hybrid genes for acyl-lipid delta(9) desaturase].
Expression of the desC gene coding for acyl-lipid delta(9) desaturase of thermophilic cyanobacterium Synechocystis sp. PCC6803 was studied in Escherichia coli cells. In a hybrid gene constructed (desC-licBM3), a sequence of the native acyl-lipid delta(9) desaturase was fused in frame with the reporter gene coding for thermostable lichenase. Lichenase contained in the hybrid protein simplified selection and analysis of the expression of membrane desaturase in the heterologous host. Comparisons of the expression for the native and hybrid genes in bacterial cells showed that lichenase remained active and thermostable in the hybrid protein, while desaturase retains the capability of introducing a double bound in the corresponding position of fatty acids.
Maali
R
R
Shimshilashvili
Kh R
KhR
Pchelkin
V P
VP
Tsydendambaev
V D
VD
Nosov
A M
AM
Los'
D A
DA
Goldenkova-Pavlova
I V
IV
D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000235:genetics; D003001:Cloning, Molecular; D000458:Cyanobacteria / Q000201:enzymology*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D044943:Fatty Acid Desaturases / Q000096:biosynthesis* / Q000235:genetics; D017930:Genes, Reporter; D006026:Glycoside Hydrolases / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000235:genetics; D013230:Stearoyl-CoA Desaturase
D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; D044943:Fatty Acid Desaturases; D013230:Stearoyl-CoA Desaturase; C029627:delta-9 fatty acid desaturase; D006026:Glycoside Hydrolases; C028020:licheninase