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Volume 148, Issue 4

Expression of the gene responds to intracellular pH and reduces the accumulation of acidic metabolic end products Free

Abstract

The YfiD protein of has been reported to be an acid-inducible protein. Here it is shown that expression of a :: reporter fusion is enhanced up to 35-fold during acidic growth. The anaerobic transcription factor FNR was confirmed as the major regulator of expression, and ArcA was found to enhance anaerobic expression, probably by displacing a repressing FNR dimer in the −935 region of the promoter. Moreover, the pyruvate sensor PdhR was shown to act as a minor anaerobic repressor of expression. On the basis of its strong homology to the C-terminal region of pyruvate formate-lyase (PFL) it was predicted that YfiD would be a radical-containing enzyme. The YfiD radical was found to be introduced by the PFL-activase enzyme, but unlike PFL, AdhE did not deactivate radicalized YfiD. The extent of radical activation of YfiD was enhanced by low intracellular pH, and thus it was concluded that both expression and YfiD activity are affected by growth at low pH. The mutant strain JRG4033 excreted increased levels of organic acids compared to the parental strain when grown in chemostat culture under oxygen-starved conditions, consistent with the acid-inducibility of expression and the recently reported ability of YfiD to rescue the activity of oxygenolytically cleaved PFL.

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Keyword(s): acid stress , dO2, dissolved oxygen tension , FNR, fumarate and nitrate reduction regulator , formate , GST, glutathione S-transferase , PFL, pyruvate formate-lyase , pH homeostasis , pyruvate formate-lyase and radical protein
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2002-04-01
2024-04-24
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Expression of the Escherichia coli yfiD gene responds to intracellular pH and reduces the accumulation of acidic metabolic end products
Microbiology 148, 1015 (2002); https://doi.org/10.1099/00221287-148-4-1015
/content/journal/micro/10.1099/00221287-148-4-1015
/content/journal/micro/10.1099/00221287-148-4-1015
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