Evidence for direct interactions between the mercuric ion transporter (MerT) and mercuric reductase (MerA) from the Tn<Emphasis Type="Italic">501</Emphasis><Emphasis Type="Italic">mer</Emphasis> operon |
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| Authors: | Mathieu Schue Kerry J Glendinning Jon L Hobman Nigel L Brown |
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| Institution: | (1) School of Biosciences, The University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK;(2) Present address: SBVME/LEMiRE, Bat 161, CEA Cadarache, Saint-Paul-Les-Durance, 13 108, France;(3) Present address: Birmingham Women’s Health Care, Metchley Park Road, Edgbaston, Birmingham, B15 2TG, UK;(4) Present address: Biotechnology and Biological Sciences Research Council, Polaris House, North Star Avenue, Swindon, SN2 1UH, UK |
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| Abstract: | Mercuric ion resistance in bacteria requires transport of mercuric ions (Hg2+) into the cytoplasmic compartment where they are reduced to the less toxic metallic mercury (Hg0) by mercuric reductase (MR). The long-established model for the resistance mechanism predicts interactions between the inner
membrane mercuric ion transporter, MerT, and the N-terminal domain of cytoplasmic MR, but attempts to demonstrate this interaction
have thus far been unsuccessful. A recently developed bacterial two-hybrid protein interaction detection system was used to
show that the N-terminal region of MR interacts with the cytoplasmic face of MerT. We also show that the cysteine residues
on the cytoplasmic face of the MerT protein are required for maximal mercuric ion transport but not for the interaction with
mercuric reductase. |
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| Keywords: | Protein– Protein interactions Mercuric ion transport Mercuric ion reductase |
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