Proteomics

Dataset Information

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Dynamics of the Escherichia coli proteome in response to the deletion of the Tat pathway


ABSTRACT: In Escherichia coli, the Twin-arginine (Tat) secretion system is one of the main routes of the protein export to the periplasm. The Tat pathway secretes a set of proteins with important physiological functions. In our study, we investigated the influence of the deactivation of the Tat pathway on the E. coli cells. We applied a comprehensive and comparative proteomic analysis of the E. coli wild type and tat mutant. This dataset provides mass spectrometry based details on the abundances of proteins in cytoplasmic, periplasmic and membrane fractions. We observed that a tat deletion increases abundances of proteins involved in protein folding, degradation, responses to heat, oxidation, osmolarity, and cold. Moreover, the impairment of E. coli outer membrane resulted in the activation of proteins responsible for cell wall biogenesis. The tat deletion negatively affects the synthesis of iron transporters and imbalances its homeostasis in the cell.

INSTRUMENT(S): Synapt MS, LTQ Orbitrap Elite

ORGANISM(S): Escherichia Coli

SUBMITTER: Katarzyna Dolata  

LAB HEAD: Katarzyna Dolata

PROVIDER: PXD008803 | Pride | 2019-02-18

REPOSITORIES: Pride

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Publications

Far-reaching cellular consequences of tat deletion in Escherichia coli revealed by comprehensive proteome analyses.

Dolata Katarzyna M KM   Montero Isabel Guerrero IG   Miller Wayne W   Sievers Susanne S   Sura Thomas T   Wolff Christian C   Schlüter Rabea R   Riedel Katharina K   Robinson Colin C  

Microbiological research 20181101


In Escherichia coli, the Twin-arginine translocation (Tat) pathway secretes a set of folded proteins with important physiological functions to the periplasm and outer membrane. The loss of Tat secretion impairs outer membrane integrity and leads to decreased cell growth. Only recently, the Tat pathway has gained more attention due to its essential role in bacterial virulence and applications in the production of fully folded heterologous proteins. In this study, we investigated the influence of  ...[more]

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