Journal
AMINO ACIDS
Volume 35, Issue 4, Pages 711-718Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-008-0053-6
Keywords
PutA; transcriptional regulation; membrane-binding; proline utilization; DNA-binding; multifunctional enzyme
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Funding
- NCRR NIH HHS [P20 RR017675, P20 RR-017675-02, P20 RR017675-057228] Funding Source: Medline
- NIGMS NIH HHS [R01 GM061068-07, R01 GM061068, GM061068] Funding Source: Medline
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The control of gene expression by enzymes provides a direct pathway for cells to respond to fluctuations in metabolites and nutrients. One example is the proline utilization A (PutA) protein from Escherichia coli. PutA is a membrane-associated enzyme that catalyzes the oxidation of L-proline to glutamate using a flavin containing proline dehydrogenase domain and a NAD(+) dependent Delta(1)-pyrroline-5-carboxylate dehydrogenase domain. In some Gram-negative bacteria such as E. coli, PutA is also endowed with a ribbon-helix-helix DNA-binding domain and acts as a transcriptional repressor of the proline utilization genes. PutA switches between transcriptional repressor and enzymatic functions in response to proline availability. Molecular insights into the redox-based mechanism of PutA functional switching from recent studies are reviewed. In addition, new results from cell-based transcription assays are presented which correlate PutA membrane localization with put gene expression levels. General membrane localization of PutA, however, is not sufficient to activate the put genes.
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