Dataset Information

Amino acid substitutions in ribosomal protein RpsU enable switching between high fitness and multiple-stress resistance in Listeria monocytogenes

ABSTRACT: A previously described low-fitness, high stress-resistant, variant of Listeria monocytogenes LO28 WT was subjected to an experimental evolution regime, selecting (in two parallel lines) for increased fitness in unstressed conditions. Evolved variants with increased fitness reverted to WT-like stress resistance. Whole genome sequencing and proteomics were used to identify differences between the ancestral and evolved strains.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Listeria Monocytogenes

SUBMITTER: Sjef Boeren

LAB HEAD: Sjef Boeren

PROVIDER: PXD022732 | Pride | 2023-10-03

REPOSITORIES: Pride

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Amino acid substitutions in ribosomal protein RpsU enable switching between high fitness and multiple-stress resistance in Listeria monocytogenes.

Koomen Jeroen J Huijboom Linda L Ma Xuchuan X Tempelaars Marcel H MH Boeren Sjef S Zwietering Marcel H MH den Besten Heidy M W HMW Abee Tjakko T

International journal of food microbiology 20210601

Microbial population heterogeneity contributes to differences in stress response between individual cells in a population, and can lead to the selection of genetically stable variants with increased stress resistance. We previously provided evidence that the multiple-stress resistant Listeria monocytogenes LO28 variant 15, carries a point mutation in the rpsU gene, resulting in an arginine-proline substitution in ribosomal protein RpsU (RpsU<sup>17Arg-Pro</sup>). Here, we investigated the trade- ...[more]

PMID: 34102570

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			Action	DRS
	MQresult_TA31-51.zip	Other
	TA31_WT_1.raw	Raw
	TA32_WT_2.raw	Raw
	TA33_WT_3.raw	Raw
	TA34_14_1_S2_1.raw	Raw