Functional Analysis of BipA in E. coli Reveals the Natural Plasticity of 50S Subunit Assembly.

ABSTRACT: BipA is a conserved translational GTPase of bacteria recently implicated in ribosome biogenesis. Here we show that Escherichia coli ΔbipA cells grown at suboptimal temperature accumulate immature large subunit particles missing several proteins. These include L17 and L17-dependent binders, suggesting that structural block 3 of the subunit folds late in the assembly process. Parallel analysis of the control strain revealed accumulation of nearly identical intermediates, albeit at lower levels, suggesting qualitatively similar routes of assembly. This came as a surprise, because earlier analogous studies of wild-type E. coli showed early binding of L17. Further investigation showed that the main path of 50S assembly differs depending on conditions of growth. Either supplementation of the med

SUBMITTER: Gibbs MR 

PROVIDER: S-EPMC7502552 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature