The functional analysis of directed amino-acid alterations in ZntR from Escherichia coli

Khan, Saira, Brocklehurst, Kathryn R., Jones, Gareth W. and Morby, Andrew P. 2002. The functional analysis of directed amino-acid alterations in ZntR from Escherichia coli. Biochemical and Biophysical Research Communications 299 (3) , pp. 438-445. 10.1016/S0006-291X(02)02660-8

Full text not available from this repository.

Abstract

The ZntR protein from Escherichia coli is a member of the MerR-family of transcriptional regulatory proteins and acts as a hyper-sensitive transcriptional switch primarily in response to Zn(II) and Cd(II). The binding of metal-ions to ZntR initiates a mechanism that remodels the cognate promoter, increasing its affinity for RNA polymerase. We have introduced site-directed mutations into zntR and shown that cysteine and histidine residues are important for transcriptional control and have an effect on metal-ion preference, sensitivity and magnitude of induction. We propose a three-dimensional model of the N-terminal region of ZntR based upon the coordinates of the MerR-family regulator BmrR.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Publisher:	Elsevier
ISSN:	0006-291X
Last Modified:	12 Nov 2019 13:20
URI:	https://orca.cardiff.ac.uk/id/eprint/62882

Citation Data

Cited 29 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item