Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	RbgA ensures the correct timing in the maturation of the 50S subunits functional sites.
Journal, issue, pages	Nucleic Acids Res, Vol. 50, Issue 19, Page 10801-10816, Year 2022
Publish date	Feb 10, 2022
Authors	Amal Seffouh / Chirstian Trahan / Tanzila Wasi / Nikhil Jain / Kaustuv Basu / Robert A Britton / Marlene Oeffinger / Joaquin Ortega /
PubMed Abstract	RbgA is an essential protein for the assembly of the 50S subunit in Bacillus subtilis. Depletion of RbgA leads to the accumulation of the 45S intermediate. A strain expressing a RbgA variant with ...RbgA is an essential protein for the assembly of the 50S subunit in Bacillus subtilis. Depletion of RbgA leads to the accumulation of the 45S intermediate. A strain expressing a RbgA variant with reduced GTPase activity generates spontaneous suppressor mutations in uL6. Each suppressor strain accumulates a unique 44S intermediate. We reasoned that characterizing the structure of these mutant 44S intermediates may explain why RbgA is required to catalyze the folding of the 50S functional sites. We found that in the 44S particles, rRNA helices H42 and H97, near the binding site of uL6, adopt a flexible conformation and allow the central protuberance and functional sites in the mutant 44S particles to mature in any order. Instead, the wild-type 45S particles exhibit a stable H42-H97 interaction and their functional sites always mature last. The dependence on RbgA was also less pronounced in the 44S particles. We concluded that the binding of uL6 pauses the maturation of the functional sites, but the central protuberance continues to fold. RbgA exclusively binds intermediates with a formed central protuberance and licenses the folding of the functional sites. Through this mechanism, RbgA ensures that the functional sites of the 50S mature last.
External links	Nucleic Acids Res / PubMed:35141754 / PubMed Central
Methods	EM (single particle)
Resolution	2.8 - 4.1 Å
Structure data	24937 7s9u EMDB-24937, PDB-7s9u: 44SR3C ribosomal particle Method: EM (single particle) / Resolution: 3.2 Å EMDB-24940: 44SR3C ribosomal particle class 2 Method: EM (single particle) / Resolution: 3.3 Å 24950 7sae EMDB-24950, PDB-7sae: 44SR70P Class1 ribosomal particle Method: EM (single particle) / Resolution: 3.0 Å EMDB-24951: 44SR70P Class2 ribosomal particle Method: EM (single particle) / Resolution: 3.0 Å EMDB-24960: The RbgA treated 44SR3C particles_Class1 Method: EM (single particle) / Resolution: 2.8 Å EMDB-24962: The RbgA treated 44SR3C particles _Class2 Method: EM (single particle) / Resolution: 2.9 Å EMDB-24965: The 44SR70P particles incubated at 37C for 15 min Class1 Method: EM (single particle) / Resolution: 3.3 Å EMDB-24966: The 44SR70P particles incubated at 37C for 15 min Class2 Method: EM (single particle) / Resolution: 3.3 Å EMDB-24967: The 44SR70P particles incubated at 37C for 15 min Class3 Method: EM (single particle) / Resolution: 3.3 Å EMDB-24971: The RbgA treated 44SR70P particles Class1 Method: EM (single particle) / Resolution: 3.1 Å EMDB-24972: The RbgA treated 44SR70P particles Class2 Method: EM (single particle) / Resolution: 3.5 Å EMDB-24973: The RbgA treated 44SR70P particles Class3 Method: EM (single particle) / Resolution: 3.2 Å EMDB-24975: The RbgA treated 44SR70P particles Class4 Method: EM (single particle) / Resolution: 4.1 Å EMDB-24977: The 45SRbgA particles incubated at 37C for 15 min Class1 Method: EM (single particle) / Resolution: 2.9 Å EMDB-24979: The 45SRbgA particles incubated at 37C for 15 min Class2 Method: EM (single particle) / Resolution: 3.0 Å EMDB-24980: The 70SR70P ribosomes Method: EM (single particle) / Resolution: 2.8 Å
Source	bacillus subtilis (bacteria)
Keywords	RIBOSOME / Ribosome assembly / 50S subunit / RbgA / YlqF / uL6 / YIqF