Freischmidt, Axel and Liss, Michael and Wagner, Ralf and Kalbitzer, Hans Robert and Horn, Godrun (2012) RNA secondary structure and in vitro translation efficiency. PROTEIN EXPRESSION AND PURIFICATION, 82 (1). pp. 26-31. ISSN 1046-5928,
Full text not available from this repository. (Request a copy)Abstract
Cell-free protein synthesis is a promising technology featuring many advantages compared to in vivo expression techniques. However, most proteins are still synthesized in vivo due to relatively low protein yields commonly achieved in vitro, especially in the batch mode of reaction. In Escherichia coli S30 extract-based cell-free systems protein yields are supposed to be partially limited by a secondary structure formation of the mRNA. In this study we checked promising members of various classes of RNA chaperones and several different RNA helicases on their ability to enhance in vitro translation. The data clearly show that the addition of none of these factors provides a general solution to the problem. However, protein yields can be increased in presence of a microRNA hybridizing with the 5' untranslated region of mRNAs, possibly by inducing structural changes improving accessibility of the Shine Dalgarno sequence for the ribosomes. (C) 2011 Elsevier Inc. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ESCHERICHIA-COLI; PROTEIN-SYNTHESIS; CHAPERONE ACTIVITY; BINDING-SITE; EXPRESSION; SYSTEM; TRANSCRIPTION; MECHANISM; HELICASES; INTRONS; Cell-free protein synthesis; S30 extract; RNA chaperone; RNA helicase; mRNA secondary structure; Micro RNA |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie III |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 19 May 2020 05:03 |
| Last Modified: | 19 May 2020 05:03 |
| URI: | https://pred.uni-regensburg.de/id/eprint/19167 |
Actions (login required)
 |
View Item |
