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Isolation and expression of CsFAD7 and CsFAD8, two genes encoding omega-3 fatty acid desaturase from Camellia sinensis

100%

Ma Q.-P. , You E. , Wang J. , Wang Y. , Ding Z.-T.

nr 09

The plastidial ω-3 fatty acid desaturase catalyses the production of trienoic fatty acids (TAs) in plant chloroplasts and plays an important role in plant responses to environmental stress. In this study, the full-length cDNAs encoding two plastidial ω-3 desaturases, designated CsFAD7 and CsFAD8 (GenBank Accession No. JX943516 and KC847167, respectively), were isolated from the tea plant (Camellia sinensis L.) using RT-PCR and RACE. Codon usage analysis revealed that U- and A-ended codons were preferentially used in these two genes. Sequence analysis showed that the deduced amino acid sequences of CsFAD7 and CsFAD8 had high homology to plastidial ω-3 desaturases from other plant species. Expression analysis by real-time PCR revealed that both genes are tissue-specific and expressed the highest levels in shoots. Meanwhile, CsFAD7 and CsFAD8 responded to various abiotic stresses and hormones, but in very different manners. Taken together, these results suggest that CsFAD7 and CsFAD8 are both responsive to abiotic stress signals; however, they may play very different roles during stress tolerance in tea plants.

Identification and characterization of the Trichoderma harzianum gene encoding alpha-1,3-glucanase involved in streptococcal mutan degradation

67%

Wiater A. , Janczarek M. , Pleszczynska M. , Szczodrak J.

nr 4

α-1,3-Glucanases (mutanases) are currently of great interest due to their potential use in the field of dental care. These enzymes have been reported in several bacteria, yeasts and fungi, but up to now, characterization of this family of proteins has been relatively poor. In this study, we identify and characterize a mutanase gene from Trichoderma harzianum CCM F-340. Sequence analysis, on the nucleotide and amino acid levels reveals that this α-1,3-glucanase is highly homologous to α-1,3-glucanases from T. harzianum isolate CBS 243.71 and T. asperellum CECT 20539. T. harzianum CCM F-340 mutanase is a 634-aa residue protein with a calculated molecular mass of 67.65 kDa, composed of two distinct, highly conserved domains (a long N-terminal catalytic domain and a short C-terminal polysaccharide-binding domain) separated by a less conserved Pro-Ser-Thr-rich linker region. The mutanase gene was expressed in an E. coli BL21(DE3) host, under the transcriptional control of T7 promoter. The purified enzyme migrated as a band of about 68 kDa after SDS-polyacrylamide gel electrophoresis, which coincided with the predicted size based on the amino acid sequence. Our data indicate that this enzyme is highly conserved in Trichoderma and can be produced in active form in such heterologous expression system.