Proteomics

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Ribosome r-protein content during stationary phase


ABSTRACT: The aim of this study was to determine the fate of ribosomes and r-proteins. In this respect, SILAC (Stable Isotope Labeled Amino acids in cell Culture) based experimental approach was used (Fig. 1). E.coli cells were grown in MOPS medium supplemented with “heavy” labeled arginine (Arg10) and lysine (Lys8). At the mid-log phase, the culture was further supplemented with a 20-fold molar excess of “light” unlabeled arginine (Arg0) and lysine (Lys0), divided into 8 aliquots, and grown for 14 days. Cell samples were collected at day one (24h), day two (48h), and subsequently in 48h intervals over the following 12 days. The ribosome particles were isolated using sucrose gradient centrifugation. the quantities of r-proteins in the 70S ribosome fraction were determined using SILAC based LC-MS/MS and normalized to the corresponding values of day one.

INSTRUMENT(S): LTQ Orbitrap XL

ORGANISM(S): Escherichia Coli

SUBMITTER: Kaspar Reier  

LAB HEAD: Tiina Tamm

PROVIDER: PXD035923 | Pride | 2023-09-01

REPOSITORIES: Pride

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Publications

A Conundrum of r-Protein Stability: Unbalanced Stoichiometry of r-Proteins during Stationary Phase in Escherichia coli.

Reier Kaspar K   Lahtvee Petri-Jaan PJ   Liiv Aivar A   Remme Jaanus J  

mBio 20220818 5


Bacterial ribosomes are composed of three rRNA and over 50 ribosomal protein (r-protein) molecules. r-proteins are essential for ribosome assembly and structural stability and also participate in almost all ribosome functions. Ribosomal components are present in stoichiometric amounts in the mature 70S ribosomes during exponential and early stationary growth phases. Ribosomes are degraded in stationary phase; however, the stability and fate of r-proteins during stationary growth phase are not kn  ...[more]

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