Purification and biochemical characterization of pullulanase type I from Thermus caldophilus GK-24 |
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Authors: | Cheorl-Ho Kim Oyekanmi Nashiru Jeong Heon Ko |
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Affiliation: | Department of Microbiology, University of Iowa, Iowa City, IA 52242, USA |
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Abstract: | Abstract We determined the relative binding affinity of the MetR protein for wild-type and mutant MetR binding sites 1 and 2 in the Escherichia coli glyA control region. The results show that MetR binding site 1 has a higher affinity for the MetR protein than binding site 2. In addition, the results suggest that binding of MetR to the glyA promoter is cooperative. Mutations that decrease the ability of MetR to bind to either site 1 or site 2 have no significant effect on MetR's ability to bend DNA. |
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Keywords: | Cooperative MetR binding DNA bending K d determination Gene activation Escherichia coli |
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