PMID:19150615

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Citation

Nord, S, Bylund, GO, Lövgren, JM and Wikström, PM (2009) The RimP protein is important for maturation of the 30S ribosomal subunit. J. Mol. Biol. 386:742-53

Abstract

The in vivo assembly of ribosomal subunits requires assistance by auxiliary proteins that are not part of mature ribosomes. More such assembly proteins have been identified for the assembly of the 50S than for the 30S ribosomal subunit. Here, we show that the RimP protein (formerly YhbC or P15a) is important for the maturation of the 30S subunit. A rimP deletion (DeltarimP135) mutant in Escherichia coli showed a temperature-sensitive growth phenotype as demonstrated by a 1.2-, 1.5-, and 2.5-fold lower growth rate at 30, 37, and 44 degrees C, respectively, compared to a wild-type strain. The mutant had a reduced amount of 70S ribosomes engaged in translation and showed a corresponding increase in the amount of free ribosomal subunits. In addition, the mutant showed a lower ratio of free 30S to 50S subunits as well as an accumulation of immature 16S rRNA compared to a wild-type strain, indicating a deficiency in the maturation of the 30S subunit. All of these effects were more pronounced at higher temperatures. RimP was found to be associated with free 30S subunits but not with free 50S subunits or with 70S ribosomes. The slow growth of the rimP deletion mutant was not suppressed by increased expression of any other known 30S maturation factor.

Links

PubMed Online version:10.1016/j.jmb.2008.12.076

Keywords

Cytoplasm/chemistry; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Deletion; Protein Biosynthesis; RNA, Ribosomal, 16S/metabolism; Ribosome Subunits, Small, Bacterial/chemistry; Ribosome Subunits, Small, Bacterial/metabolism; Temperature

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