Wurm, Jan Philip (2021) Assignment of the Ile, Leu, Val, Met and Ala methyl group resonances of the DEAD-box RNA helicase DbpA from E. coli. BIOMOLECULAR NMR ASSIGNMENTS, 15. pp. 121-128. ISSN 1874-2718, 1874-270X
Full text not available from this repository. (Request a copy)Abstract
ATP-dependent DEAD-box helicases constitute one of the largest families of RNA helicases and are important regulators of most RNA-dependent cellular processes. The functional core of these enzymes consists of two RecA-like domains. Changes in the interdomain orientation of these domains upon ATP and RNA binding result in the unwinding of double-stranded RNA. The DEAD-box helicase DbpA from E. coli is involved in ribosome maturation. It possesses a C-terminal RNA recognition motif (RRM) in addition to the canonical RecA-like domains. The RRM recruits DbpA to nascent ribosomes by binding to hairpin 92 of the 23S rRNA. To follow the conformational changes of Dbpa during the catalytic cycle we initiated solution state NMR studies. We use a divide and conquer approach to obtain an almost complete resonance assignment of the isoleucine, leucine, valine, methionine and alanine methyl group signals of full length DbpA (49 kDa). In addition, we also report the backbone resonance assignments of two fragments of DbpA that were used in the course of the methyl group assignment. These assignments are the first step towards a better understanding of the molecular mechanism behind the ATP-dependent RNA unwinding process catalyzed by DEAD-box helicases.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | CRYSTAL-STRUCTURE; COOPERATIVE BINDING; PROTEIN; ATP; DEAD-box helicase; Ribosome assembly; RNA; Methyl group assignment |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Petra Gürster |
| Date Deposited: | 21 Apr 2021 13:41 |
| Last Modified: | 21 Apr 2021 13:41 |
| URI: | https://pred.uni-regensburg.de/id/eprint/43174 |
Actions (login required)
 |
View Item |
