Biofunction-assisted DNA detection through RNase H-enhanced 3′ processing of a premature tRNA probe in a wheat germ extract

Ogawa, Atsushi; Tabuchi, Junichiro; Doi, Yasunori; Takamatsu, Masashi

doi:10.1016/j.bmcl.2016.05.091

Cited by 4 publications

(3 citation statements)

References 37 publications

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“…97 The same design was later adapted by Ogawa et al to develop sup-tRNA switches triggered by complementary DNA oligonucleotides in WGE. 98 More recently, Ogawa and colleagues manipulated a viral translation initiation mechanism mediated by the 3 0 capindependent translation element (3 0 CITE) from barley yellow dwarf virus (BYDV). The viral RNA element located in the 3 0 UTR activates translation by forming a kissing loop interaction with another element located in the 5 0 UTR, mimicking the canonical 5 0 cap-3 0 poly(A) interaction mediated by eukaryotic translation initiation factors (eIFs).…”

Section: Other Mechanismsmentioning

confidence: 99%

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Cell-free riboswitches

Tabuchi

Yokobayashi

2021

RSC Chem. Biol.

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Section: Other Mechanismsmentioning

confidence: 99%

“… 97 The same design was later adapted by Ogawa et al to develop sup-tRNA switches triggered by complementary DNA oligonucleotides in WGE. 98 …”

Section: Eukaryotic Cell-free Riboswitchesmentioning

confidence: 99%

Cell-free riboswitches

Tabuchi

Yokobayashi

2021

RSC Chem. Biol.

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“…This enabled the development of a paper-based diagnostic assay for the detection of Ebola (Pardee et al, 2014), a concept that could be extended to the development of more sensitive rapid tests for other infectious diseases suitable for use in developing countries or testing water quality (Jung et al, 2020) with a simple assay (Grawe et al, 2019;Thavarajah et al, 2020). It is a promising approach to combine DNA detection with the expression of a marker protein, which will enable new concepts for biosensor developments (Duyen et al, 2016;Ogawa et al, 2016;Zhang et al, 2020). For such applications, the translation system could also be miniaturized or used in a fluidic array device (Jackson et al, 2015) for automation and easy use.…”

Section: Introductionmentioning

confidence: 99%

Easy Synthesis of Complex Biomolecular Assemblies: Wheat Germ Cell-Free Protein Expression in Structural Biology

Fogeron

Lecoq

Cole

et al. 2021

Front. Mol. Biosci.

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Cell-free protein synthesis (CFPS) systems are gaining more importance as universal tools for basic research, applied sciences, and product development with new technologies emerging for their application. Huge progress was made in the field of synthetic biology using CFPS to develop new proteins for technical applications and therapy. Out of the available CFPS systems, wheat germ cell-free protein synthesis (WG-CFPS) merges the highest yields with the use of a eukaryotic ribosome, making it an excellent approach for the synthesis of complex eukaryotic proteins including, for example, protein complexes and membrane proteins. Separating the translation reaction from other cellular processes, CFPS offers a flexible means to adapt translation reactions to protein needs. There is a large demand for such potent, easy-to-use, rapid protein expression systems, which are optimally serving protein requirements to drive biochemical and structural biology research. We summarize here a general workflow for a wheat germ system providing examples from the literature, as well as applications used for our own studies in structural biology. With this review, we want to highlight the tremendous potential of the rapidly evolving and highly versatile CFPS systems, making them more widely used as common tools to recombinantly prepare particularly challenging recombinant eukaryotic proteins.

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