NDLI: Evidence for direct interactions between the mercuric ion transporter (MerT) and mercuric reductase (MerA) from the Tn501 mer operon

Content Provider	Springer Nature Link
Author	Schue, Mathieu Glendinning, Kerry J. Hobman, Jon L. Brown, Nigel L.
Copyright Year	2007
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.
Starting Page	107
Ending Page	116
Page Count	10
File Format	PDF
ISSN	09660844
Journal	BioMetals
Volume Number	21
Issue Number	2
e-ISSN	15728773
Language	English
Publisher	Springer Netherlands
Publisher Date	2007-04-25
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Protein–Protein interactions Mercuric ion transport Mercuric ion reductase Physical Chemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences

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