Expression and purification of recombinant thermostable DNA-binding protein <i>Sso7d</i>-Reference-Cited by-同舟云学术

Expression and purification of recombinant thermostable DNA-binding protein <i>Sso7d</i>

Published:2023-09-04 Issue:3 Volume:59 Page:225-233
ISSN:2524-2342
Container-title:Proceedings of the National Academy of Sciences of Belarus, Chemical Series
language:
Short-container-title:Vescì Akademìì navuk Belarusì. Seryâ himičnyh navuk

Author:

Sachanka A. B.¹,Trawkina M.¹,Shchur V. V.¹,Usanov S. A.¹,Yantsevich A. V.¹

Affiliation:

1. Institute of Bioorganic Chemistry of the National Academy of Sciences of Belarus

Abstract

The Sso7d protein has exceptional structural stability and the ability to bind highly specifically to DNA, which makes the protein a promising module for creating fusion proteins and test systems. Sso7d is a part of fusion high-fidelity DNA polymerases capable of carrying out the polymerase chain reaction even in the presence of PCR inhibitors. Application of faster, simpler, and more efficient method for protein production will significantly reduce the cost of creating biosensors and conducting analyzes. This paper describes a new efficient method for obtaining recombinant Sso7d protein with a high degree of purity without using affinity chromatography.

Publisher

Publishing House Belorusskaya Nauka

Subject

Inorganic Chemistry,Organic Chemistry,Chemistry (miscellaneous),Analytical Chemistry

Reference21 articles.

1. Baumann H., Knapp S., Lundbäck T., Ladenstein R., Härd T. Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus. Nature Structure Biology, 1994, vol. 1, no. 11, pp. 808‒819. https://doi.org/10.1038/nsb1194-808

2. Luscombe N. M., Austin S. E., Berman H. M., Thornton J. M. An overview of the structures of protein-DNA complexes. Genome Biology, 2000, vol. 1, no. 1. https://doi.org/10.1186/gb-2000-1-1-reviews001

3. Consonni R., Santomo L., Fusi P., Tortora P., Zetta L. A single-point mutation in the extreme heat- and pressure-resistant sso7d protein from sulfolobus solfataricus leads to a major rearrangement of the hydrophobic core. Biochemistry, 1999, vol. 38, no. 39, pp. 12709‒12717. https://doi.org/10.1021/bi9911280

4. Consonni R., Arosio I., Belloni B., Fogolari F., Fusi P., Shehi E., Zetta L. Investigations of Sso7d catalytic residues by NMR titration shifts and electrostatic calculations. Biochemistry, 2003, vol. 42, no. 6, pp. 1421‒1429. https://doi.org/10.1021/bi0265168

5. Granata V., Vecchio P. D., Barone G., Shehi E., Fusi P., Tortora P., Graziano G. Guanidine-induced unfolding of the Sso7d protein from the hyperthermophilic archaeon Sulfolobus solfataricus. International Journal of Biological Macromolecules, 2004, vol. 34, no. 3, pp. 195‒201. https://doi.org/10.1016/j.ijbiomac.2004.04.002