Skip to main content

Research Repository

Advanced Search

Characterisation of a putative AraC transcriptional regulator from Mycobacterium smegmatis

Evangelopoulos, D; Gupta, A; Lack, N A; Maitra, A; Ten Bokum, A M C; Kendall, S L; Sim, E; Bhakta, S


D Evangelopoulos

A Gupta

N A Lack

A Maitra

A M C Ten Bokum

S L Kendall

E Sim

S Bhakta


MSMEG_0307 is annotated as a transcriptional regulator belonging to the AraC protein family and is located adjacent to the arylamine N-acetyltransferase (nat) gene in Mycobacterium smegmatis, in a gene cluster, conserved in most environmental mycobacterial species. In order to elucidate the function of the AraC protein from the nat operon in M. smegmatis, two conserved palindromic DNA motifs were identified using bioinformatics and tested for protein binding using electrophoretic mobility shift assays with a recombinant form of the AraC protein. We identified the formation of a DNA:AraC protein complex with one of the motifs as well as the presence of this motif in 20 loci across the whole genome of M. smegmatis, supporting the existence of an AraC controlled regulon. To characterise the effects of AraC in the regulation of the nat operon genes, as well as to gain further insight into its function, we generated a ?araC mutant strain where the araC gene was replaced by a hygromycin resistance marker. The level of expression of the nat and MSMEG_0308 genes was down-regulated in the ?araC strain when compared to the wild type strain indicating an activator effect of the AraC protein on the expression of the nat operon genes.


Evangelopoulos, D., Gupta, A., Lack, N. A., Maitra, A., Ten Bokum, A. M. C., Kendall, S. L., …Bhakta, S. (2014). Characterisation of a putative AraC transcriptional regulator from Mycobacterium smegmatis. Tuberculosis, 94(6), 664-671.

Journal Article Type Article
Acceptance Date Sep 1, 2014
Publication Date Sep 28, 2014
Deposit Date Nov 11, 2014
Publicly Available Date Feb 28, 2019
Print ISSN 1472-9792
Publisher Elsevier
Peer Reviewed Peer Reviewed
Volume 94
Issue 6
Pages 664-671
Public URL
Additional Information Corporate Creators : Birkbeck College, Oxford


You might also like

Downloadable Citations