NMR resonance assignments of RNase P protein from Thermotoga maritima

作者：Zeng Danyun; Brown Benjamin P; Voehler Markus W; Cai Sheng; Reiter Nicholas J^*

来源：Biomolecular NMR Assignments, 2018, 12(1): 183-187.

DOI：10.1007/s12104-018-9806-7

• NMR resonance assignment
• Thermatoga maritima
• RNase P
• Protein-tRNA binding
• Ribonucleoprotein
• TALOS-N prediction

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 H-1, C-13, and N-15 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.

• 出版日期2018-4