Authors

A. Naganathan; M. P. Wood;S. D. Moore

Comments

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Abbreviated Journal Title

PLoS One

Keywords

ELONGATION-FACTOR-P; AMINOACYL-TRANSFER-RNA; ESCHERICHIA-COLI; TRANSLATION ELONGATION; QUALITY-CONTROL; IN-VIVO; STRUCTURAL INSIGHTS; CRYSTAL-STRUCTURE; INITIATION-FACTOR; ESSENTIAL GTPASE; Multidisciplinary Sciences

Abstract

The loss of the large ribosomal protein L9 causes a reduction in translation fidelity by an unknown mechanism. To identify pathways affected by L9, we identified mutants of E. coli that require L9 for fitness. In a prior study, we characterized L9-dependent mutations in the essential GTPase Der (EngA). Here, we describe a second class of L9-dependent mutations that either compromise or inactivate elongation factor P (EF-P, eIF5A in eukaryotes). Without L9, Delta efp cells are practically inviable. Cell fractionation studies revealed that, in both the Der and EF-P mutant cases, L9's activity reduces immature 16S rRNA in 30S particles and partially restores the abundance of monosomes. Inspired by these findings, we discovered that L9 also enhances 16S maturation in wild-type cells. Surprisingly, although the amount of immature 16S in 30S particles was found to be elevated in Delta rplI cells, the amount in polysomes was low and inversely correlated with the immature 16S abundance. These findings provide an explanation for the observed fitness increases afforded by L9 in these mutants and reveal particular physiological conditions in which L9 becomes critical. Additionally, L9 may affect the partitioning of small subunits containing immature 16S rRNA.

Journal Title

Plos One

Volume

10

Issue/Number

4

Publication Date

1-1-2015

Document Type

Article

Language

English

First Page

23

WOS Identifier

WOS:000353016500005

ISSN

1932-6203

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