The Sulfur Oxidation Operon Repressor Function is Influenced by the Product of its Adjacent Upstream ORF in <Emphasis Type="Italic">Pseudaminobacter salicylatoxidans</Emphasis> KCT001 |
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Authors: | Email author" target="_blank">Sukhendu?MandalEmail author |
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Institution: | (1) The Waksman Institute, 190 Frelinghuysen Road, Piscataway, NJ 08854-8020, USA |
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Abstract: | The repressor of sulfur-oxidizing (sox) operon regulates expression of genes encoding a multienzyme complex that governs the chemolithotrophic sulfur oxidation
in Pseudaminobacter salycylatoxidans KCT001. The inducer of sox operon viz., thiosulfate and other sulfur anions had no impact on in vitro repressor–operator interaction which indicates an atypical
derepression mechanism. The reduced repressor has higher affinity for its operator DNA. The sulfur oxidation repressor binds
with operator regions and led to efficient repression in trans, however, increased repressor concentration resulted in higher gene expression. Using a reporter system in E. coli, the present study established that the thioredoxin-like protein, encoded in immediate upstream ORF, could nullify the observed
reversal of the repression at higher repressor concentration. In this context, the involvement of the upstream gene product
in the regulation of the sulfur oxidation gene expression has been reported. |
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Keywords: | |
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