Brody Frink
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Brody Frink has a total of 11 co-authors. Here are the top co-authors by number of shared publications:
Bastian Oldenkott
Institut für Zelluläre und Molekulare Botanik, Abteilung Molekulare Evolution, University of Bonn, Bonn, Germany
1 shared publicationChristian G. Feiler
Helmholtz-Zentrum Berlin für Materialien und Energie, Macromolecular Crystallography, Berlin, Germany
1 shared publicationDaniil Verbitskiy
Molekulare Botanik, Universität Ulm, Ulm, Germany
1 shared publication- Gert Weber
Macromolecular Crystallography, Helmholtz-Zentrum Berlin für Materialien und Energie, Berlin, Germany
1 shared publication - Gottfried J. Palm
Department Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany
1 shared publication - Manfred Stefan Weiss
Macromolecular Crystallography, Helmholtz-Zentrum Berlin, Albert-Einstein-Strasse 15, 12489 Berlin, Germany
1 shared publication
Latest Publications
- Open Access
- 21 June 2021
- Published by Springer Nature in Nature Catalysis
- Vol. 4 (6) , 510-522
DYW domain structures imply an unusual regulation principle in plant organellar RNA editing catalysis
RNA editosomes selectively deaminate cytidines to uridines in plant organellar transcripts—mostly to restore protein functionality and consequently facilitate mitochondrial and chloroplast function. The RNA editosomal pentatricopeptide repeat proteins serve target RNA recognition, whereas the intensively studied DYW domain elicits catalysis. Here we present structures and functional data of a DYW domain in an inactive ground state and activated. DYW domains harbour a cytidine deaminase fold and a C-terminal DYW motif, with catalytic and structural zinc atoms, respectively. A conserved gating domain within the deaminase fold regulates the active site sterically and mechanistically in a process that we termed gated zinc shutter. Based on the structures, an autoinhibited ground state and its activation are cross-validated by RNA editing assays and differential scanning fluorimetry. We anticipate that, in vivo, the framework of an active plant RNA editosome triggers the release of DYW autoinhibition to ensure a controlled and coordinated cytidine deamination playing a key role in mitochondrial and chloroplast homeostasis.
- 21 June 2021
- Published by Springer Nature in Nature Catalysis
- Vol. 4 (6) , 510-522
Open AccessDYW domain structures imply an unusual regulation principle in plant organellar RNA editing catalysis
RNA editosomes selectively deaminate cytidines to uridines in plant organellar transcripts—mostly to restore protein functionality and consequently facilitate mitochondrial and chloroplast function. The RNA editosomal pentatricopeptide repeat proteins serve target RNA recognition, whereas the intensively studied DYW domain elicits catalysis. Here we present structures and functional data of a DYW domain in an inactive ground state and activated. DYW domains harbour a cytidine deaminase fold and a C-terminal DYW motif, with catalytic and structural zinc atoms, respectively. A conserved gating domain within the deaminase fold regulates the active site sterically and mechanistically in a process that we termed gated zinc shutter. Based on the structures, an autoinhibited ground state and its activation are cross-validated by RNA editing assays and differential scanning fluorimetry. We anticipate that, in vivo, the framework of an active plant RNA editosome triggers the release of DYW autoinhibition to ensure a controlled and coordinated cytidine deamination playing a key role in mitochondrial and chloroplast homeostasis.