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Articles

Expression analysis of squalene synthase gene in mevalonate pathway of Sanghuangporus baumii

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Pages 176-183 | Received 06 Oct 2021, Accepted 29 Mar 2022, Published online: 10 Apr 2022

Figures & data

Table 1. List of primers used in the study.

Figure 1. Sequence analysis of SbSQS and its promoter region. (A) Exon and intron sites of SbSQS. (B) Phylogenetic analysis of SQS from S. baumii and other species. (C) Functional elements of the SbSQS promoter.

Figure 1. Sequence analysis of SbSQS and its promoter region. (A) Exon and intron sites of SbSQS. (B) Phylogenetic analysis of SQS from S. baumii and other species. (C) Functional elements of the SbSQS promoter.

Table 2. Origins of homologous amino-acid sequences.

Figure 2. Sequence alignment of the 12 amino acid sequences of SQS from the indicated species. Homology level was highlighted by shading in color: black for 100%, pink for ≥ 75% and blue for ≥ 50% identity. Conserved functional segments (A, B and C) are framed in red.

Figure 2. Sequence alignment of the 12 amino acid sequences of SQS from the indicated species. Homology level was highlighted by shading in color: black for 100%, pink for ≥ 75% and blue for ≥ 50% identity. Conserved functional segments (A, B and C) are framed in red.

Figure 3. Analysis of the secondary structure and predicted three-dimensional structure of SbSQS. (A) The predicted transmembrane regions of SbSQS. (B) Annotation of the secondary structure of SbSQS. (C) Predicted three-dimensional structure of SbSQS.

Figure 3. Analysis of the secondary structure and predicted three-dimensional structure of SbSQS. (A) The predicted transmembrane regions of SbSQS. (B) Annotation of the secondary structure of SbSQS. (C) Predicted three-dimensional structure of SbSQS.

Figure 4. Heterologous expression of SbSQS in E. coli following IPTG induction (1 mmol/L). The bands indicated by the red arrow are target proteins. Lane M, protein molecular weight markers; Lane 1, blank control group: E. coli harboring empty vector; Lane 2–7, E. coli harboring pET-32a-SbSQS induced by IPTG at 0 h, 2 h, 4 h, 6 h, 8 h, 10 h.

Figure 4. Heterologous expression of SbSQS in E. coli following IPTG induction (1 mmol/L). The bands indicated by the red arrow are target proteins. Lane M, protein molecular weight markers; Lane 1, blank control group: E. coli harboring empty vector; Lane 2–7, E. coli harboring pET-32a-SbSQS induced by IPTG at 0 h, 2 h, 4 h, 6 h, 8 h, 10 h.

Figure 5. Biomass and triterpenoid contents during S. baumii fermentation.

Figure 5. Biomass and triterpenoid contents during S. baumii fermentation.

Figure 6. Relative expression level of SbSQS during S. baumii fermentation. The values with * are significantly different (p < 0.05).

Figure 6. Relative expression level of SbSQS during S. baumii fermentation. The values with * are significantly different (p < 0.05).
Supplemental material

Supplemental Material

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Data availability statement

All data that support the findings reported in this study are available from the corresponding author upon reasonable request.