Homo-trimeric structure of the ribonuclease for rRNA processing, FAU-1, from Pyrococcus furiosus

• Published in: Journal of biochemistry (Tokyo)
• Main Authors: Kawai, Gota, Okada, Kiyoshi, Baba, Seiki, Sato, Asako, Sakamoto, Taiichi, Kanai, Akio
• Format: Journal Article
• Language: English
• Published: England 01.02.2024
• Subjects: X-ray crystallography; Pyrococcus furiosus; RNase E; Alphafold2; rRNA processing
• ISSN: 1756-2651
• DOI: 10.1093/jb/mvae010

Crystal structure of a ribonuclease for rRNA processing, FAU-1, from Pyrococcus furiosus was determined with the resolution of 2.57 Å in a homo-trimeric form. The monomer structure consists of two domains, N-terminal and C-terminal domains. C-terminal domain forms trimer and each N-terminal domain locates outside of the trimer core. In the obtained crystal, a dinucleotide, pApUp, was bound to the N-terminal domain, indicating that N-terminal domain has the RNA-binding ability. The affinities to RNA of FAU-1 and a fragment corresponding to the N-terminal domain, FAU-ΔC, were confirmed by PAGE and NMR. Interestingly, well dispersed NMR signals were observed at 318 K, indicating that the FAU-ΔC-F18 complex form an ordered structure at higher temperature. As predicted in our previous works, FAU-1 and RNase E show a structural similarity in their RNA binding regions. However, structural similarity between RNase E and FAU-1 could be found in the limited regions of the N-terminal domain. On the other hand, structural similarity between C-terminal domain and some proteins including a phosphatase was found. Thus, it is possible that the catalytic site is located in C-terminal domain.