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- Title
Homo-trimeric structure of the ribonuclease for rRNA processing, FAU-1, from Pyrococcus furiosus.
- Authors
Kawai, Gota; Okada, Kiyoshi; Baba, Seiki; Sato, Asako; Sakamoto, Taiichi; Kanai, Akio
- Abstract
Crystal structure of a ribonuclease for ribosomal RNA 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 polyacrylamide gel electrophoresis and nuclear magnetic resonance (NMR). Interestingly, well-dispersed NMR signals were observed at 318K, indicating that the FAU-ΔC–F18 complex form an ordered structure at higher temperature. As predicted in our previous works, FAU-1 and ribonuclease (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.
- Subjects
PYROCOCCUS furiosus; RIBONUCLEASES; RIBOSOMAL RNA; NUCLEAR magnetic resonance; PHOSPHOPROTEIN phosphatases; POLYACRYLAMIDE gel electrophoresis
- Publication
Journal of Biochemistry, 2024, Vol 175, Issue 6, p671
- ISSN
0021-924X
- Publication type
Article
- DOI
10.1093/jb/mvae010