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| | ==Solution structure of the C-terminal domain of S. aureus Hibernating Promoting Factor (CTD-SaHPF)== | | ==Solution structure of the C-terminal domain of S. aureus Hibernating Promoting Factor (CTD-SaHPF)== |
| - | <StructureSection load='5nko' size='340' side='right' caption='[[5nko]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='5nko' size='340' side='right'caption='[[5nko]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nko]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NKO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NKO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nko]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NKO FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hpf, SAOUHSC_00767 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93061 STAA8])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nko OCA], [http://pdbe.org/5nko PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nko RCSB], [http://www.ebi.ac.uk/pdbsum/5nko PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nko ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5nko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nko OCA], [https://pdbe.org/5nko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nko RCSB], [https://www.ebi.ac.uk/pdbsum/5nko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nko ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HPF_STAA8 HPF_STAA8]] Required for dimerization of active 70S ribosomes into 100S ribosomes; when added to monomeric 70S ribosomes stimulates formation of 100S dimeric ribosomes. Unlike E.coli, 100S ribosomes are present during exponential growth, peak during early stationary phase and then decrease (shown for strain NBRC 3060).[HAMAP-Rule:MF_00839]<ref>PMID:20015224</ref> | + | [https://www.uniprot.org/uniprot/HPF_STAA8 HPF_STAA8] Required for dimerization of active 70S ribosomes into 100S ribosomes; when added to monomeric 70S ribosomes stimulates formation of 100S dimeric ribosomes. Unlike E.coli, 100S ribosomes are present during exponential growth, peak during early stationary phase and then decrease (shown for strain NBRC 3060).[HAMAP-Rule:MF_00839]<ref>PMID:20015224</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Staa8]] | + | [[Category: Large Structures]] |
| - | [[Category: Ayupov, R K]] | + | [[Category: Staphylococcus aureus subsp. aureus NCTC 8325]] |
| - | [[Category: Khusainov, I S]] | + | [[Category: Ayupov RK]] |
| - | [[Category: Kieffer, B]] | + | [[Category: Khusainov IS]] |
| - | [[Category: Usachev, K S]] | + | [[Category: Kieffer B]] |
| - | [[Category: Validov, S Z]] | + | [[Category: Usachev KS]] |
| - | [[Category: Yusupov, M M]] | + | [[Category: Validov SZ]] |
| - | [[Category: Hibernating promoting factor]]
| + | [[Category: Yusupov MM]] |
| - | [[Category: Hibernation]]
| + | |
| - | [[Category: Hpf]]
| + | |
| - | [[Category: Pathogen]]
| + | |
| - | [[Category: Ribosomal protein]]
| + | |
| - | [[Category: Ribosome]]
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| - | [[Category: Staphylococcus aureus]]
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| Structural highlights
Function
HPF_STAA8 Required for dimerization of active 70S ribosomes into 100S ribosomes; when added to monomeric 70S ribosomes stimulates formation of 100S dimeric ribosomes. Unlike E.coli, 100S ribosomes are present during exponential growth, peak during early stationary phase and then decrease (shown for strain NBRC 3060).[HAMAP-Rule:MF_00839][1]
Publication Abstract from PubMed
In bacteria, ribosomal hibernation shuts down translation as a response to stress, through reversible binding of stress-induced proteins to ribosomes. This process typically involves the formation of 100S ribosome dimers. Here, we present the structures of hibernating ribosomes from human pathogen Staphylococcus aureus containing a long variant of the hibernation-promoting factor (SaHPF) that we solved using cryo-electron microscopy. Our reconstructions reveal that the N-terminal domain (NTD) of SaHPF binds to the 30S subunit as observed for shorter variants of HPF in other species. The C-terminal domain (CTD) of SaHPF protrudes out of each ribosome in order to mediate dimerization. Using NMR, we characterized the interactions at the CTD-dimer interface. Secondary interactions are provided by helix 26 of the 16S ribosomal RNA We also show that ribosomes in the 100S particle adopt both rotated and unrotated conformations. Overall, our work illustrates a specific mode of ribosome dimerization by long HPF, a finding that may help improve the selectivity of antimicrobials.
Structures and dynamics of hibernating ribosomes from Staphylococcus aureus mediated by intermolecular interactions of HPF.,Khusainov I, Vicens Q, Ayupov R, Usachev K, Myasnikov A, Simonetti A, Validov S, Kieffer B, Yusupova G, Yusupov M, Hashem Y EMBO J. 2017 Jul 14;36(14):2073-2087. doi: 10.15252/embj.201696105. Epub 2017 Jun, 23. PMID:28645916[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ueta M, Wada C, Wada A. Formation of 100S ribosomes in Staphylococcus aureus by the hibernation promoting factor homolog SaHPF. Genes Cells. 2010 Jan;15(1):43-58. doi: 10.1111/j.1365-2443.2009.01364.x. Epub, 2009 Dec 15. PMID:20015224 doi:http://dx.doi.org/10.1111/j.1365-2443.2009.01364.x
- ↑ Khusainov I, Vicens Q, Ayupov R, Usachev K, Myasnikov A, Simonetti A, Validov S, Kieffer B, Yusupova G, Yusupov M, Hashem Y. Structures and dynamics of hibernating ribosomes from Staphylococcus aureus mediated by intermolecular interactions of HPF. EMBO J. 2017 Jul 14;36(14):2073-2087. doi: 10.15252/embj.201696105. Epub 2017 Jun, 23. PMID:28645916 doi:http://dx.doi.org/10.15252/embj.201696105
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