Document Type
Article
Language
eng
Publication Date
2-15-2018
Publisher
Springer
Source Publication
Biomolecular NMR Assignments
Source ISSN
1874-2718
Abstract
Ribonuclase P (RNase P) is an essential metallo-endonuclease that catalyzes 5′ precursor-tRNA (ptRNA) processing and exists as an RNA-based enzyme in bacteria, archaea, and eukaryotes. In bacteria, a large catalytic RNA and a small protein component assemble to recognize and accurately cleave ptRNA and tRNA-like molecular scaffolds. Substrate recognition of ptRNA by bacterial RNase P requires RNA-RNA shape complementarity, intermolecular base pairing, and a dynamic protein-ptRNA binding interface. To gain insight into the binding specificity and dynamics of the bacterial protein-ptRNA interface, we report the backbone and side chain 1H, 13C, and 15N resonance assignments of the hyperthermophilic Thermatoga maritima RNase P protein in solution at 318 K. Our data confirm the formation of a stable RNA recognition motif (RRM) with intrinsic heterogeneity at both the N- and C-terminus of the protein, consistent with available structural information. Comprehensive resonance assignments of the bacterial RNase P protein serve as an important first step in understanding how coupled RNA binding and protein-RNA conformational changes give rise to ribonucleoprotein function.
Recommended Citation
Zeng, Danyun; Brown, Benjamin P.; Voehler, Markus W.; Cai, Sheng; and Reiter, Nicholas J., "NMR resonance assignments of RNase P protein from Thermotoga maritima" (2018). Chemistry Faculty Research and Publications. 1006.
https://epublications.marquette.edu/chem_fac/1006
Comments
Accepted version. Biomolecular NMR Assignments, Vol. 12 (February 15, 2018): 183-187. DOI. © 2018 Springer. Used with permission.