NMR assignments of the N-terminal domain of Staphylococcus aureus hibernation promoting factor (SaHPF).
Biomol NMR Assign. 2017 Oct 04;:
Authors: Usachev KS, Ayupov RK, Validov SZ, Khusainov IS, Yusupov MM
Abstract
Staphylococcus aureus: hibernation-promoting factor (SaHPF) is a 22.2*kDa stationary-phase protein that binds to the ribosome and turns it to the inactive form favoring survival under stress. Sequence analysis has shown that this protein is combination of two homolog proteins obtained in Escherichia coli-ribosome hibernation promoting factor (HPF) (11,000*Da) and ribosome modulation factor RMF (6500*Da). Binding site of E. coli HPF on the ribosome have been shown by X-ray study of Thermus thermophilus ribosome complex. Hence, recent studies reported that the interface is markedly different between 100S from S. aureus and E. coli. Cryo-electron microscopy structure of 100S S. aureus ribosomes reveal that the SaHPF-NTD binds to the 30S subunit as observed for shorter variants of HPF in other species and the C-terminal domain (CTD) protrudes out of each ribosome in order to mediate dimerization. SaHPF-NTD binds to the small subunit similarly to its homologs EcHPF, EcYfiA, and a plastid-specific YfiA. Furthermore, upon binding to the small subunit, the SaHPF-NTD occludes several antibiotic binding sites at the A site (hygromycin B, tetracycline), P site (edeine) and E site (pactamycin, kasugamycin). In order to elucidate the structure, dynamics and function of SaHPF-NTD from S. aureus, here we report the backbone and side chain resonance assignments for SaHPF-NTD. Analysis of the backbone chemical shifts by TALOS+ suggests that SaHPF-NTD contains two ?-helices and four ?-strands (?1-?1-?2-?3-?4-?2 topology). Investigating the long-term survival of S. aureus and other bacteria under antibiotic pressure could lead to advances in antibiotherapy.
PMID: 28980143 [PubMed - as supplied by publisher]
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NMR assignments of the N-terminal domain of Staphylococcus aureus hibernation promoting factor (SaHPF).
Linear Mode
