Effect of expansion of Shine-Dalgarno sequence for overexpression of nicotinamide adenine dinucleotide oxidase gene from Deinococcus geothermalis in Escherichia coli

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Published Jul 29, 2023
DOI: https://doi.org/10.18103/mra.v11i7.2.4172

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Main Article Content

Masahide Ishikawa
Department of Life Science and Green Chemistry, Faculty of Engineering, Saitama Institute of Technology, Fukaya 3690293, Japan.

Abstract

Thermostable enzymes have applications in biosensors and bioreactors. Overexpression of thermostable enzyme-encoding genes from thermophiles in Escherichia coli is necessary to produce sufficient quantities of such enzymes. Deinococcus gerthermalis is a moderately thermophilic bacterium and has moderately thermostable enzymes. Nicotinamide adenine dinucleotide (NADH) is an important coenzyme for various dehydrogenases. NADH oxidase (Nox) catalyze the oxidation of NADH. Therefore, Nox is a versatile enzyme that can be used in combination with many types of biosensors. This study reveals the effect of expansion of the SD sequence in the leader sequence of NADH oxidase gene from D. geothermalis for overexpression in E. coli, and shows that while 1- or 2-bases expansion of the Shine-Dalgarno sequence is effective. This study should be contributed to the expression of many genes in E. coli.

Keywords: nicotinamide adenine dinucleotide oxidase gene, Deinococcus geothermalis, Escherichia coli, E. coli

Article Details

How to Cite
ISHIKAWA, Masahide. Effect of expansion of Shine-Dalgarno sequence for overexpression of nicotinamide adenine dinucleotide oxidase gene from Deinococcus geothermalis in Escherichia coli. Medical Research Archives, [S.l.], v. 11, n. 7.2, july 2023. ISSN 2375-1924. Available at: <https://esmed.org/MRA/mra/article/view/4172>. Date accessed: 16 may 2024. doi: https://doi.org/10.18103/mra.v11i7.2.4172.
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Issue
Vol 11 No 7.2 (2023): July Issue, Vol.11, Issue 7.2
Section
Research Articles

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References

1. Updike S.J, Hicks G.P, The enzyme embodied electrode. Nature, 1967; 214, 986.

2. Schchiri M, Kawamori R, Yamasaki Y, Hakui N, Abe H, Wearable artificial endocrine pancreas with needle-type glucose sensor. Lancet. 1982; 320, 1129-1131.

3. Higuchi M, Shimada M, Matsumoto J, Yamamoto Y, Rhaman A, Kamio Y. Molecular cloning and sequence analysis of the gene encoding the H2O2-forming NADH oxidase from Streptococcus mutans. Biosci. Biotechnol. Biochem. 1994; 58, 1603–1607.

4. Creanga C, Murr N.E, Development of new disposable NADH biosensors based on NADH oxidase. J. Electroanal. Chem. 2011; 656, 179-184.

5. Tabata M, Koushima F, Totani M, Use of a biosensor consisting of an immobilized NADH oxidase column and a hydrogen peroxide electrode for the determination of serum lactate dehydrogenase activity. Alal. Chem. Acta 1994; 298(1), 113-119.

6. Suzuki S, Matsumura N, Ohoka T, Sakuma S, Nakamura T, Ishikawa M, Important sequence for overexpression of NADH oxidase gene from Thermus thermophilus HB8 in Escherichia coli. J. Environ. Sci. 2009; Suppl 1, S105-107.

7. Ferreira A.C, Nobre M.F, Rainey F.A, Silva M.T., Wait R, Burghardt J, Chung A.P, Da Costa M.S, Deinococcus geothermalis sp. nov. and Deinococcus murrayi sp. nov., Two Extremely Radiation-Resistant and Slightly Thermophilic Species from Hot Springs. Int. J. Syst. Bacteriol. 1997; 47(4), 939–947.

8. Sase K, Iwasaki T, Karasawa H, Ishikawa M, Overexpression of NADH oxidase gene from Deinococcus geothermalis in Escherichia coli. J. Environ. Sci. 2013; 25(Suppl.), S169-171.

9. Shine D, Dalgarno L, The 3‘-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA 1974; 71, 1342-1346.

10. Lee K, Holland-Staley C.A, Cunningham P.R, Genetic analysis of the Shine-Dalgarno interaction: selection of alternative functional mRNA-rRNA combinations. RNA 1996; 2(12), 1270-1285.

11. Leberman R, Antonsson B, Giovanelli R, Guariguata R, Schumann R, Wittinghofer A, A simplified procedure for the isolation of bacterial polypeptide elongation factor EF-Tu. Anal. Biochem. 1980; 104, 29–36.

12. Hengen P, Purification of His-Tag fusion proteins from Escherichia coli. Trends biochem. Sci. 1995; 20(7): 285--286.

13. de Smit, M.H, van Duin, J, Secondary structure of the ribosome binding site determines translational efficiency: a quantitative analysis. Proc. Natl. Acad. Sci. USA. 1990; 87, 7668–7672.

14. Yin J, Bao L, Tian H, Gao X, Yao W, Quantitative relationship between the mRNA secondary structure of translational initiation region and the expression level of heterologous protein in Eschrichia coli. J. Ind. Microbiol. Biotechnol. 2016; 43(1), 97-102.