Proteomics

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Functional analysis of BipA in E. coli reveals the plasticity of 50S ribosome assembly

ABSTRACT: BipA is a conserved translational GTPase that resembles elongation factor EF-G and 30S assembly factor LepA. Recent evidence suggests that BipA functions in 50S subunit assembly, but the precise role of the factor remains unclear. Here, we use stable isotope labeling of amino acids in culture and mass spectrometry (SILAC / MS) to examine the function of BipA in ribosome biogenesis. During growth at suboptimal temperature, loss of BipA leads to accumulation of immature large subunit particles (~40S) that lack several proteins. These include L2, L7/12, L10, L14, L16, L17, L19, L27, L28 and L32. Parallel analysis of the control (wild-type) strain shows accumulation of virtually identical intermediate particles, although at much lower levels. Further analysis showed that the main path of 50S assembly differs depending on media in which the cells are grown, demonstrating the robust and flexible nature of the assembly process.

INSTRUMENT(S): Bruker Daltonics instrument model

ORGANISM(S): Escherichia Coli

SUBMITTER: Jenny Moon  

LAB HEAD: Kurt L. Fredrick

PROVIDER: PXD017917 | Pride | 2021-09-09

REPOSITORIES: Pride

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Dataset's files

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Action DRS
A_KurtbipArep1txt.rar Other
A_KurtbipArep2txt.rar Other
A_KurtbipArep3txt.rar Other
A_bipAset1data.rar Other
A_bipAset2data.rar Other
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Publications

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

Gibbs Michelle R MR   Moon Kyung-Mee KM   Warner Benjamin R BR   Chen Menglin M   Bundschuh Ralf R   Foster Leonard J LJ   Fredrick Kurt K  

Journal of molecular biology 20200722 19

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, su  ...[more]

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