Abstract
The ribosome is a large ribonucleoprotein complex that synthesizes protein in all living organisms. Ribosome biogenesis is a complex process that requires synchronization of various cellular events, including ribosomal RNA (rRNA) transcription, ribosome assembly, and processing and post-transcriptional modification of rRNA. Ribosome biogenesis is fine-tuned with various assembly factors, possibly including nucleotide modification enzymes. Ribosomal small subunit pseudouridine synthase A (RsuA) pseudouridylates U516 of 16S helix 18. Protein RsuA is a multi-domain protein that contains the N-terminal peripheral domain, which is structurally similar to the ribosomal protein S4. Our study shows RsuA preferably binds and pseudouridylates an assembly intermediate that is stabilized by ribosomal protein S17 over the native-like complex. In addition, the N-terminal domain truncated RsuA showed that the presence of the S4-like domain is important for RsuA substrate recognition.
Highlights
Ribosomes are ribonucleoprotein complexes that synthesize proteins in all living organisms
Various trans-acting factors are required to maintain the synchronicity of these various processes and increase the efficiency and accuracy of ribosome biogenesis. 16S ribosomal RNA (rRNA) is modified sequentially from 5 –3 direction while the ribosome assembly is in progress
The FRET signal gradually increased and reached a maximum of ~0.03 when Ribosomal small subunit pseudouridine synthase A (RsuA) was added, indicating the ability of RsuA to bind to 30S 5 -domain rRNA, even in the absence of r-proteins (Figure 2B)
Summary
Ribosomes are ribonucleoprotein complexes that synthesize proteins in all living organisms. Modification enzymes responsible for pseudouridine (Ψ) and m7G at positions 516 and 527 (Escherichia coli numbering) in the 5 -domain can bind to early assembly intermediates, influence the association of late-binding r-proteins. Ribosomal small subunit pseudouridine synthase A (RsuA) modifies the U516 of 16S rRNA. Hdomweavinerd, eSl4e-tliiokne mdoumtaanitnodferliebtoiosnommaul tlanrgteosfurbibuonsiotmpsaeluladroguerisduibnuensiytnptsheausdeoCu(rRidluinCe)ssyhnotwhaesdetCha(tRtlhueCe)nszhyomweeids tshtiallt cthapeaebnlzeypmseeuidsosutirlildcyalpaatibolne pevseundwoiuthrioduytlathtieonpreevsencwe iotfhtohuet Sth4-elipkreedseonmcaeionf[t1h2e].ST4h-leikSe4-dliokme adionm[1a2in]. These growth defects could be Biomolecules 2020, 10, 841 disadvantage against wild type E. coli strains [14] These growth defects could be reversed by replacing the wild type RluD and TruB with non-functional mutants, suggesting far more important roles for those PUS enzymes than their enzymatic activity [15]. Many rRNA PUS enzymes may have roles other than pseudouridylation, likely related to ribosome biogenesis. The importance of RsuA peripheral domain in the binding of the RsuA is discussed
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