Journal of Molecular Biology
CommunicationThe Effect of Ribosome Assembly Cofactors on In Vitro 30S Subunit Reconstitution
Section snippets
Acknowledgements
This work was supported by a grant from the National Institutes of Health (R37-GM-53757) to J.R.W. and by the Skaggs Institute for Chemical Biology. P.M.W. was supported by the Carl Trygger Foundation. The authors thank Prof. Gary Siuzdak and Dr. Sunia Trauger of the Scripps Center for Mass Spectrometry for advice and access to instrumentation. Gunter Stier is gratefully acknowledged for providing plasmid pETM10, Dr. Michael T. Sykes for mass spectrometry data analysis programs, and Dr. Zahra
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2019, Journal of Biological ChemistryCitation Excerpt :In their study, RimP was only found in the fractions of 30S subunit but not others in sucrose gradient centrifugation, and primer extension studies demonstrated that RimP knockout bacteria up-regulated the level of pre-16S rRNA but down-regulated mature 16S rRNA levels (4). Recently, quantitative MS studies on E. coli suggested that RimP can increase the binding kinetics of the S5 and S12 ribosomal proteins to the 5′ domain of rRNA in vitro (7). In addition, it was reported that the relative timing of the assembly of the 3′ domain and the formation of the central pseudoknot structure in the 16S rRNA depend on the presence of the assembly factor RimP (8).