Abstract
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 Δ1-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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Acknowledgments
This work is a contribution of the University of Nebraska Agricultural Research Division, supported in part by funds provided through the Hatch Act. This research was supported by grants from the National Institutes of Health GM061068 and the National Science Foundation MCB0340912. This publication was also made possible by NIH Grant Number P20 RR-017675-02 from the National Center for Research Resources. Its contents are solely the responsibility of the authors and do not necessarily represent the official views of the NIH.
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Zhou, Y., Zhu, W., Bellur, P.S. et al. Direct linking of metabolism and gene expression in the proline utilization A protein from Escherichia coli . Amino Acids 35, 711–718 (2008). https://doi.org/10.1007/s00726-008-0053-6
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DOI: https://doi.org/10.1007/s00726-008-0053-6