Rise of the terminator protein tus: A versatile tool in the biotechnologist's toolbox.
Autor: | Toft CJ; Molecular and Cell Biology, College of Public Health, Medical and Veterinary Sciences, James Cook University, Douglas, QLD, 4811, Australia., Sorenson AE; Molecular and Cell Biology, College of Public Health, Medical and Veterinary Sciences, James Cook University, Douglas, QLD, 4811, Australia., Schaeffer PM; Molecular and Cell Biology, College of Public Health, Medical and Veterinary Sciences, James Cook University, Douglas, QLD, 4811, Australia. Electronic address: patrick.schaeffer@jcu.edu.au. |
---|---|
Jazyk: | angličtina |
Zdroj: | Analytica chimica acta [Anal Chim Acta] 2022 Jun 22; Vol. 1213, pp. 339946. Date of Electronic Publication: 2022 May 16. |
DOI: | 10.1016/j.aca.2022.339946 |
Abstrakt: | Tus is a protein involved in DNA replication termination that binds specific DNA sequences (Ter) located around the terminus region of the chromosome in Enterobacterales. Tus and Ter form a unique monomeric protein-DNA complex which is one of strongest of its kind. A fascinating aspect of Tus-Ter is its ability to dramatically change conformation into a locked structure upon progression of a replication fork towards the non-permissive face of the complex. Over the last two decades, several new technologies have emerged harnessing the unique and interesting properties of this fascinating DNA-binding protein. This review highlights the important properties of the Tus-Ter complex and their exploitation for the development of diverse and novel ultrasensitive detection devices as well as innovative genomic and proteomic platform technologies. A variety of ex vivo and in vivo bioanalytical applications are discussed, including immuno-PCR diagnostic, bioassay and protein array technologies that are broadly relevant to the fields of cancer biology, microbiology and immunology. A perspective on future research and applications is provided. (Copyright © 2022 Elsevier B.V. All rights reserved.) |
Databáze: | MEDLINE |
Externí odkaz: |