AI Article Synopsis
- SaHPF is a factor in Staphylococcus aureus that promotes the formation of 100S ribosome dimers, allowing the bacteria to conserve energy in tough conditions.* -
- The study determined the crystal structure of the C-terminal domain of SaHPF at high resolution, revealing how the dimer interface is arranged.* -
- Mutations in specific residues at the dimer interface of SaHPF were shown to prevent ribosome dimerization, highlighting their critical role in the process.*
Article Abstract
Staphylococcus aureus hibernation promoting factor (SaHPF) is responsible for the formation of 100S ribosome dimers, which in turn help this pathogen to reduce energy spent under unfavorable conditions. Ribosome dimer formation strongly depends on the dimerization of the C-terminal domain of SaHPF (CTD). In this study, we solved the crystal structure of CTD at 1.6 Å resolution and obtained a precise arrangement of the dimer interface. Residues Phe, Val, Thr, Ile, Tyr, Ile andThr in the dimer interface of SaHPF protein were mutated and the effects were analyzed for the formation of 100S disomes of ribosomes isolated from S. aureus. It was shown that substitution of any of single residues Phe, Val, Ile, Tyr and Ile in the SaHPF homodimer interface abolished the ribosome dimerization in vitro.
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| http://dx.doi.org/10.1016/j.jsb.2019.107408 | DOI Listing |
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