Correction

Proteomic analysis of differential protein expression in Acidithiobacillus ferrooxidans cultivated in high potassium concentration (vol 168, pg 455, 2013)

Journal

MICROBIOLOGICAL RESEARCH
Volume 182, Issue -, Pages 163-168

Publisher

ELSEVIER GMBH
DOI: 10.1016/j.micres.2015.02.004

Keywords

Acidithiobacillus ferrooxidans; Potassium ion response; Two-dimensional electrophoresis; Glycocalyx; ATP synthase

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Acidithiobacillus ferrooxidans is a chemolithoautotrophic acidophile that oxidizes ferrous iron or sulfur compounds to obtain energy in the presence of various ions. To investigate the potassium ion response of A. ferrooxidans, we conducted a proteomics analysis. We identified eight proteins that were differentially expressed in the presence of high potassium concentration, including four up-regulated and four down-regulated proteins. Transcription levels of the genes encoding differential expressed proteins were subsequently analyzed by Northern blot in the presence of high potassium concentration. Among the up-regulated proteins, GDP-mannose 4,6-dehydratase, ribose 5-phosphate isomerase A and ribosephosphate pyrophosphokinase were known to be implicated in the synthesis of glycocalyx, suggesting that the formation of glycocalyx might be involved in the A. ferrooxidans response to high potassium concentration. Thickening of the glycocalyx layer was also observed in cells cultivated under high potassium concentration via transmission electronic microscopy (TEM) analysis. Among the down-regulated proteins, ATP synthase Fl delta subunit and ATP synthase Fl beta subunit were two important components of ATP synthase. ATP synthase (P-ATPase) is directly linked to the transport of potassium into the cell, thus Acidithiobacillus ferrooxidans might just reduce the quantity of ATP synthase to offset the high potassium level in the culture medium. Therefore, the results obtained here provide some new clues to improve our understanding of the response of A. ferrooxidans to high potassium concentration. (C) 2015 Elsevier GmbH. All rights reserved.

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